God’s Holy Crosses from the Tree of Life versus Laminin Cross from the Lutheran blood

What is the difference between Man-made Laminin and the Entactin/Nidogen glycoproteins and molecular structure of the Laminin Schematic drawing of a cross versus God’s Purple Royal molecular structurally stable Neutron Crosses within the prismatic stationary nucleus or centriole of the centrosomes?

First and foremost, a man-made schematic drawing of a cross should never represent cDNA cloning of a human embryo pluripotent stem cell that is compounded with a mouse embryo fibroblast or epithelial tissue resulting fifteen different chains of Laminin and used as feeder cells. Feeder cells are ingredients used in food and beverage products, pharmaceutical medicine or transfection and transduction virus implantation in any organism including humans, but also as a flavor enhancer in coffee creamers, dairy products, and fast-food chain restaurant products.

Secondly, today and the past 8 decades science has become very evil using their theories about Gene inheritance, DNA/RNA gene sequences of harmful nucleotides as our true evolutionary genetics. That we were created from cyanobacteria, apes, animals or petrochemicals as our original blood line is outrageous! The Illuminates have deceived so many people into believing their science creation is to help you when it clearly induces harm! Their true mission is to accomplish depopulation, diseases and cancer to collect from your health insurance plan empowering their bank accounts. While you suffer physically and financially!

Thirdly, God is our true Evolutionary Creator! God makes is truly clear who he is through Immortal Genetics and Molecules in a TREE. The Tree of LIFE byproducts that were all steam distilled with high heat, and the molecular structure did not dissipate, quite the opposite it is colorful vibrant and shows many two- and three-dimensional Genetic structured images. The Immortal and or Primitive molecules are retained and analyzed through micrographs from a digital camera inserted in one of the binocular lenses in a simple novel microscope. The glass slide of each byproduct of liquid or centrifuged powder, or gum resin sample was placed under a 4x objective lens using a10x wide field equaling a 40-x magnification. As mentioned in my document named the Tree of Life rare and non-conventional scientific analysis that these evaluations are exceedingly rare compared to traditional science analysis.

The Tree of Life micrographs or images that you are now seeing shows one Immortal X-shaped Metastate Chromsome of rainbow colors, Prismatic Centrosomes and Centrioles with Royal PURPLE CROSSES, right angles, and a few square shapes within the nucleus of the primitive and Prismatic Luminous Centriole. Royal Purple is God’s color but the CROSS and many Crosses seen is his legendary symbol!

We all know what the Cross means, Jesus was crucified on the cross to redeem our sins. He is our Savior, Protector and Defender! Everything about the “Tree of Life” Immortal Genetics of God’s Neutron or Neutral Agents and Hematopoietic Stem Cells, Myelin Sheathing, Myelinated Axons, Brain Neurons of Purkinje and Pyramidal neurons within the byproducts are here to heal and repair us from the damage the medical industry created with their pharmaceutical poisons and implanted viruses through vaccines, food and beverages. It is also to give us courage, confidence, truth and facts, and establish a loving relationship with God!

Unlike the Satanic Illuminates who harm us with lies and propaganda with their vaccines or implanted viruses or virions, scientific experimentations, pharmaceutical drugs, preservatives in our food and beverages, air, water, and soil pollution all from toxic and carcinogenic petrochemicals as well as DNA/RNA or deoxygenated nucleic acids and ribonucleic acids. The nucleotides comprise the four fundamental building blocks as a nitrogenous base with a phosphate and sugar backbone!

Lastly, the major structural difference between Laminin and God’s Royal Purple Crosses is the byproducts from the Tree of Life are not made from in vivo and in vitro cloning of human embryo pluripotent stem cells or mouse embryo fibroblast (tissue) processes, but also no biomarkers or trackers, stains, dyes, heat fixing or green fluorescent proteins of any toxic chemical poison were used to magnify, enhance, or illuminate the cells or molecules! Additionally, the micrographs are real images, not done through (png files) of schematic or graphic drawings or animated figures as the Illuminati’s and their Scientist who worship them create!

Please read the paragraphs below on the Functions of Laminin– The Illuminati scientists proudly announce Laminin is the Lutheran blood of glycoproteins. It is disgusting!

The Truth and Facts are here you can choose to hear it or forbear it, it is always your choice!!!!

Secondly, Laminins are a family of glycoproteins from the extracellular matrix – such as all connective epithelial lining tissue of organs, stroma cells structural cells, and digestive tissue etc.

So, scientists, and many companies are implanting virions or viruses (recombinant DNA or Retroviruses) through transfection and transduction processes using messenger RNA (mRNA), which binds at the Nitrogen terminal end also known as the downstream 3’ foot untranslated region or 3’UTR primed region. The 3’UTR is the binding site where the promoter is activated and transcribes or copies a single strand from the conserved double stranded DNA. The single strand of the DNA is activated with more polymerized concentrated gene sequences nucleotides in the upstream direction toward the 5’foot- untranslated region or 5’UTR region of the Carbon terminal entrance. When the carboxylic acid is removed due to more toxic phosphorylation, methanol and ethanol chemical bonding to the carbon and nitrogen atoms it is now called amides (carboxamide group). This is an operon or cluster of gene polypeptide fragments because stem cells are our dividers, and regulators and cleave the foreign invaders, pathogens, and polypeptides.

The Repressor is the silencer, inhibitor, translator and alternator and can even block the white blood cells (hematopoietic stem cells) from defending or protecting our extracellular regions. Additionally, prevent chemical homeostasis, induce coagulation within lymphatic system of the mucous membrane and neuroglandular, create vasoconstriction within the cardiovascular circuits, and demyelinate our nerve fiber insulator severely impacting our central nervous system. Their transfection and transduction implanted virions or recombinant DNA retroviruses in our medicine or taken as immunized vaccines at birth and preschool has been the decline and demise of worldwide health through genocide bioweapons. The embryo or fetal tissue organisms in our food, beverages, medicine, and vaccines. IS Truly DISQUSTING! By inhibiting or repressing our powerful mitochondria ATP or adenine triphosphate biological energy through the pancreas hormone called insulin which breaks down or degrades glucose (carbohydrates and sugars) is the main target to produce many cascading diseases and cancers.

At the 3’UTR a removal of gene sequence or nucleoside occurs. The removal is called an Intron. The nucleic acid removed was Thymine at the N-Terminal going upstream towards the Carbon terminal end another removal of an RNA or ribonucleic acid occurs and this removal is called Extron, in which could be a carbonyl group (methanol or ethanol) or methyl group- (methane) through a continuous conjugative or redox chemical process known as methylation or demethylation!

In chemistry, the removal of a compound is called an elimination reaction. In molecular biology, it is called Introns and Extron’s. The binding site is called a Promotor in molecular biology. While the binding site in Chemistry is called a covalent bond at linear, branched, side chains or cyclic rings producing a chemical structural formula of chemical compounds and functional groups.

The Illuminates created such a deception through terminology and confusion even in separate fields of science!

Laminins are a family of glycoproteins of the extracellular matrix of all animals.

Glycoproteins- are proteins which contain oligosaccharide chains covalently attached to amino acid side chains. The carbohydrate is attached to the protein in a translational or posttranslational modification through a process known as glycosylation. Secreted extracellular proteins are often glycosylated.

There are fifteen chains of Laminin that have been identified in vivo and

The major difference between the Human Entactin also known as nidogen: cDNA cloning, cellular expression, and mapping of the gene to chromosome

https://en.wikipedia.org/wiki/Fibroblast

Use of fibroblasts as feeder cells

Mouse embryonic fibroblasts (MEFs) are often used as supportive “feeder cells” in research using human embryonic stem cells,^[10] induced pluripotent stem cells and primary epithelial cell culture.^[11] However, many researchers are trying to phase out MEFs in favor of culture media with precisely defined ingredients in order to facilitate the development of clinical-grade products.^[12]

 12. Hynds, R.E.; Bonfanti, P.; Janes, S.M. (2018). “Regenerating human epithelia with cultured stem cells: feeder cells, organoids and beyond”. EMBO Molecular Medicine. 10 (2): 139–150.

What Are Feeder Cells – Reproduction Online (reproduction-online.org)

In view of the potential clinical applications of stem cell-derived tissues or primary epithelial cells, the use of human fibroblasts as an alternative to MEF feeders has been studied.^[13] Whereas the fibroblasts are usually used to maintain pluripotency of the stem cells, they can also be used to facilitate development of the stem cells into specific type of cells such as cardiomyocytes.^[14]

9.  Silzle T, Randolph GJ, Kreutz M, Kunz-Schughart LA (January 2004). “The fibroblast: sentinel cell and local immune modulator in tumor tissue”. International Journal of Cancer. 108 (2): 173–180. doi:10.1002/ijc.11542. PMID14639599. S2CID10936034.
10. ^ Bonnans C, Chou J, Werb Z (December 2014). “Remodelling the extracellular matrix in development and disease”. Nature Reviews. Molecular Cell Biology. 15 (12): 786–801. doi:10.1038/nrm3904. PMC4316204. PMID25415508.
11. ^ Llames, S.; García-Pérez, E.; Meana, A.; Larcher, F.; del Río, M. (2015). “Feeder Layer Cell Actions and Applications”. Tissue Eng Part B Rev. 21 (4): 345–353. doi:10.1089/ten.teb.2014.0547. PMC4533020. PMID25659081.
12. ^ Hynds, R.E.; Bonfanti, P.; Janes, S.M. (2018). “Regenerating human epithelia with cultured stem cells: feeder cells, organoids and beyond”. EMBO Molecular Medicine. 10 (2): 139–150. doi:10.15252/emmm.201708213. PMC5801505. PMID29288165.
13. ^ Hagbard, L.; Cameron, K.; August, P.; Penton, C.; Parmar, M.; Hay, D.C.; Kallur, T. (2018). “Developing defined substrates for stem cell culture and differentiation”. Philosophical Transactions of the Royal Society B. 373 (1750). doi:10.1098/rstb.2017.0230. PMC5974452. PMID29786564.
14. ^Desai N, Rambhia P, Gishto A (February 2015). “Human embryonic stem cell cultivation: historical perspective and evolution of xeno-free culture systems”. Reproductive Biology and Endocrinology. 13 (1): 9. doi:10.1186/s12958-015-0005-4. PMC4351689. PMID25890180.
15. ^ Matsuda Y, Takahashi K, Kamioka H, Naruse K (September 2018). “Human gingival fibroblast feeder cells promote maturation of induced pluripotent stem cells into cardiomyocytes”. Biochemical and Biophysical Research Communications. 503 (3): 1798–1804. doi:10.1016/j.bbrc.2018.07.116. PMID30060947.

https://en.wikipedia.org/wiki/Laminin#/media/File:Laminin111.png

By Gad Armony – Own work, CC BY-SA 4.0, https://commons.wikimedia.org/w/index.php?curid=62526469

Illustration of the laminin-111 complex depicting the domain organization.

Gad Armony – Own work

An Illustration of the Laminin-111 complex

• CC BY-SA 4.0
• File:Laminin111.png
• Created: 27 March 2017
• Uploaded: 18 September 2017

https://pubmed.ncbi.nlm.nih.gov/2119632

Entactin: structure and function – PubMed (nih.gov)

Entactin: structure and function

Abstract

Entactin is an integral and ubiquitous component of the basement membrane. The amino acid sequences of the mouse and human molecules have been determined and exhibit 85% sequence identity. The molecule is organized into three structural domains, an N-terminal globule (I) is linked to a smaller C-terminal globule (III) by a rigid stalk (II) largely consisting of cysteine-rich EGF-like homology repeats and a cysteine-rich thyroglobulin homology repeat. The molecule binds calcium ions and supports cell adhesion. However, its major function may be the assembly of the basement membrane. The carboxyl globule binds tightly to one of the short arms of laminin at the inner rodlike segment. This same region is also believed to be responsible for the attachment of entactin to type IV collagen at approximately 80 nm from its carboxyl noncollagenous end. Entactin therefore could serve as a bridge between the two most abundant molecules in the basement membrane. Supporting evidence for this role has been obtained from transfection of human choriocarcinoma, JAR, cells with the entactin gene. JAR cells synthesize laminin and type IV collagen but not entactin. Transfection of entactin into the cells stimulated incorporation of laminin and type IV collagen along with entactin into the extracellular matrix and into structures resembling focal contacts. The calcium-binding activity of entactin may play a role in the matrix assembly process. The protease sensitivity of entactin suggests that it may be a target for proteolytic activity during tissue remodeling, metastasis, and other events requiring the turnover of the basement membrane.

https://pubmed.ncbi.nlm.nih.gov/8507559

Embryonal carcinoma and the basement membrane glycoproteins laminin and entactin

A E Chung ¹

Affiliations expand

• PMID: 8507559

Abstract

The mouse embryonal carcinoma lines PCC4-F and F9 have played important roles in the isolation and characterization of the two ubiquitous basement membrane proteins, laminin and entactin. The contributions of these cells to our work on extracellular matrices are briefly summarized. The in vitro differentiation of PCC4-F gives rise to a multiplicity of cell types. Two of these cell types have been propagated as cell lines. One of these, M1536-B3, synthesizes and deposits copious quantities of extracellular matrix glycoproteins, which led to the initial discovery and characterization of laminin and entactin. In addition, M1536-B3 provides a model system for analyzing the assembly of laminin and the laminin-entactin complex and for manipulating extracellular matrix structure and composition. The other cell line, 4CQ, synthesizes a matrix consisting of fibronectin and entactin. F9 cells differentiate to endodermal cells in response to retinoic acid and dibutyryl cyclic AMP (Strickland and Mahdavi, Cell 15: 393-402, 1978). The differentiated cells synthesize basement membrane components and provide the probes for the cDNA cloning of entactin and the three chains of laminin. The F9 cells have been widely employed to examine the regulation of expression of the laminin and entactin genes.

https://en.wikipedia.org/wiki/Laminin

Laminin

Illustration of the laminin-111 complex depicting the domain organization.

Parts of this article (those related to Pathology) need to be updated. The reason given is: Improve the article with up-to-date research on the topic. Please help update this article to reflect recent events or newly available information. (October 2023)

Laminins are a family of glycoproteins of the extracellular matrix of all animals. They are major constituents of the basement membrane, namely the basal lamina (the protein network foundation for most cells and organs). Laminins are vital to biological activity, influencing cell differentiation, migration, and adhesion.^[1][2]

Laminins are heterotrimeric proteins with a high molecular mass (~400 to ~900 kDa) and possess three different chains (α, β and γ) encoded by five, four, and three paralogous genes in humans, respectively. The laminin molecules are named according to their chain composition, e.g. laminin-511 contains α5, β1, and γ1 chains.^[3] Fourteen other chain combinations have been identified in vivo. The trimeric proteins intersect, composing a cruciform structure that is able to bind to other molecules of the extracellular matrix and cell membrane.^[4] The three short arms have an affinity for binding to other laminin molecules, conducing sheet formation. The long arm is capable of binding to cells and helps anchor organized tissue cells to the basement membrane.

Laminins are integral to the structural scaffolding of almost every tissue of an organism—secreted and incorporated into cell-associated extracellular matrices. These glycoproteins are imperative to the maintenance and vitality of tissues; defective laminins can cause muscles to form improperly, leading to a form of muscular dystrophy, lethal skin blistering disease (junctional epidermolysis bullosa), and/or defects of the kidney filter (nephrotic syndrome).^[5]

Laminin Types

In humans, fifteen laminin trimers have been identified. The laminins are combinations of different alpha-, beta-, and gamma-chains.^[6]

• Five alpha-chain isoforms: LAMA1, LAMA2, LAMA3 (which has three splice forms), LAMA4, LAMA5
• Four beta-chain isoforms: LAMB1, LAMB2, LAMB3, LAMB4 (note that no known laminin trimer incorporates LAMB4 and its function remains poorly understood)
• Three gamma-chain isoforms: LAMC1, LAMC2, LAMC3

Laminins were previously numbered as they were discovered, i.e. laminin-1, laminin-2, laminin-3, etc., but the nomenclature was changed to describe which chains are present in each isoform (laminin-111, laminin-211, etc.).^[3] In addition, many laminins had common names before either laminin nomenclature was in place.^[7][8]

Old nomenclature	Old synonyms	Chain composition	New nomenclature
Laminin-1	EHS laminin	α1β1γ1	Laminin-111
Laminin-2	Merosin	α2β1γ1	Laminin-211
Laminin-3	S-laminin	α1β2γ1	Laminin-121
Laminin-4	S-merosin	α2β2γ1	Laminin-221
Laminin-5 / Laminin-5A	Kalinin, epiligrin, nicein, ladsin	α3Aβ3γ2	Laminin-332 / Laminin-3A32
Laminin-5B		α3Bβ3γ2	Laminin-3B32
Laminin-6 / Laminin-6A	K-laminin	α3Aβ1γ1	Laminin-311 / Laminin-3A11
Laminin-7 / Laminin-7A	KS-laminin	α3Aβ2γ1	Laminin-321 / Laminin-3A21
Laminin-8		α4β1γ1	Laminin-411
Laminin-9		α4β2γ1	Laminin-421
Laminin-10	Drosophila-like laminin	α5β1γ1	Laminin-511
Laminin-11		α5β2γ1	Laminin-521
Laminin-12		α2β1γ3	Laminin-213
Laminin-14		α4β2γ3	Laminin-423
		α5β2γ2	Laminin-522
Laminin-15		α5β2γ3	Laminin-523

Function

Laminins form independent networks and are associated with type IV collagen networks via entactin,^[9] fibronectin,^[10] and perlecan. The proteins also bind to cell membranes through integrins and other plasma membrane molecules, such as the dystroglycan glycoprotein complex and Lutheran blood group glycoprotein.^[4] Through these interactions, laminins critically contribute to cell attachment and differentiation, cell shape and movement, maintenance of tissue phenotype, and promotion of tissue survival.^[4][6] Some of these biological functions of laminin have been associated with specific amino-acid sequences or fragments of laminin.^[4] For example, the peptide sequence [GTFALRGDNGDNGQ], which is located on the alpha-chain of laminin, promotes the adhesion of endothelial cells.^[11]

Laminin alpha4 is distributed in a variety of tissues including peripheral nerves, dorsal root ganglion, skeletal muscle and capillaries; in the neuromuscular junction, it is required for synaptic specialization.^[12] The structure of the laminin-G domain has been predicted to resemble that of pentraxin.^[13]

Role in neural development

Laminin-111 is a major substrate along which nerve axons will grow, both in vivo and in vitro. For example, it lays down a path that developing retinal ganglion cells follow on their way from the retina to the tectum. It is also often used as a substrate in cell culture experiments. The presence of laminin-1 can influences how the growth cone responds to other cues. For example, growth cones are repelled by netrin when grown on laminin-111 but are attracted to netrin when grown on fibronectin.^{[citation needed]} This effect of laminin-111 probably occurs through a lowering of intracellular cyclic AMP.^{[citation needed]}

Role in peripheral nerve repair

Laminins are enriched at the lesion site after peripheral nerve injury and are secreted by Schwann cells. Neurons of the peripheral nervous system express integrin receptors that attach to laminins and promote neuroregeneration after injury.^[14]

Pathology

Dysfunctional structure of one particular laminin, laminin-211, is the cause of one form of congenital muscular dystrophy.^[15] Laminin-211 is composed of an α2, β1 and γ1 chains. This laminin’s distribution includes the brain and muscle fibers. In muscle, it binds to alpha-dystroglycan and integrin alpha7—beta1 via the G domain, and via the other end, it binds to the extracellular matrix.

Abnormal laminin-332, which is essential for epithelial cell adhesion to the basement membrane, leads to a condition called junctional epidermolysis bullosa, characterized by generalized blisters, exuberant granulation tissue of skin and mucosa, and pitted teeth.

Malfunctional laminin-521 in the kidney filter causes leakage of protein into the urine and nephrotic syndrome.^[5]

Role in cancer

Some of the laminin isoforms have been implicated in cancer pathophysiology. The majority of transcripts that harbor an internal ribosome entry site (IRES) are involved in cancer development via corresponding proteins. A crucial event in tumor progression referred to as epithelial to mesenchymal transition (EMT) allows carcinoma cells to acquire invasive properties. The translational activation of the extracellular matrix component laminin B1 (LAMB1) during EMT has been recently reported suggesting an IRES-mediated mechanism. In this study, the IRES activity of LamB1 was determined by independent bicistronic reporter assays. Strong evidences exclude an impact of cryptic promoter or splice sites on IRES-driven translation of LamB1. Furthermore, no other LamB1 mRNA species arising from alternative transcription start sites or polyadenylation signals were detected that account for its translational control. Mapping of the LamB1 5′-untranslated region (UTR) revealed the minimal LamB1 IRES motif between -293 and -1 upstream of the start codon. Notably, RNA affinity purification showed that the La protein interacts with the LamB1 IRES. This interaction and its regulation during EMT were confirmed by ribonucleoprotein immunoprecipitation. In addition, La was able to positively modulate LamB1 IRES translation. In summary, these data indicate that the LamB1 IRES is activated by binding to La which leads to translational upregulation during hepatocellular EMT.^[16]

Use in cell culture

Together with other major components of the ECM, such as collagens and fibronectin, laminins have been used to enhance mammalian cell culture, especially in the case of pluripotent stem cells, as well as some primary cell cultures, which can be difficult to propagate on other substrates. Two types of naturally-sourced laminins are commercially available. Laminin-111 extracted from mouse sarcomas is one popular laminin type, as well as laminin mixtures from human placenta, which may primarily correspond to laminin-211, 411 or 511, depending on the provider.^[17] The various laminin isoforms are practically impossible to isolate from tissues in pure form due to extensive cross-linking and the need for harsh extraction conditions, such as proteolytic enzymes or low pH, that cause degradation. Therefore, recombinant laminins have been produced since the year 2000.^[18] This made it possible to test if laminins could have a significant role in vitro as they have in the human body. In 2008, two groups independently showed that mouse embryonic stem cells can be grown for months on top of recombinant laminin-511.^[19][20] Later, Rodin et al. showed that recombinant laminin-511 can be used to create a totally xeno-free and defined cell culture environment to culture human pluripotent ES cells and human iPS cells.^[21]

https://en.wikipedia.org/wiki/Nidogen-1

Nidogen-1 (NID-1), formerly known as entactin, is a protein that in humans is encoded by the NID1 gene.^[5][6] Both nidogen-1 and nidogen-2 are essential components of the basement membrane alongside other components such as type IV collagen, proteoglycans (heparan sulfate and glycosaminoglycans), laminin^[7] and fibronectin.^[8]

Function

Nidogen-1 is a member of the nidogen family of basement membrane glycoproteins. The protein interacts with several other components of basement membranes. Structurally it (along with perlecan) connects the networks formed by collagens and laminins to each other.^[9] It may also play a role in cell interactions with the extracellular matrix.^[10][11]

Clinical significance

Mutations in NID1 cause autosomal dominant Dandy–Walker malformation with occipital encephalocele (ADDWOC).^[12][13]

Interactions

Nidogen-1 has been shown to interact with FBLN1.^[14][15][16]

References

1. ^ Jump up to:^a b c GRCh38: Ensembl release 89: ENSG00000116962 – Ensembl, May 2017
2. ^ Jump up to:^a b c GRCm38: Ensembl release 89: ENSMUSG00000005397 – Ensembl, May 2017
3. ^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
4. ^ “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ Olsen DR, Nagayoshi T, Fazio M, Mattei MG, Passage E, Weil D, Timpl R, Chu ML, Uitto J (June 1989). “Human nidogen: cDNA cloning, cellular expression, and mapping of the gene to chromosome Iq43”. Am. J. Hum. Genet. 44 (6): 876–85. PMC1715653. PMID2471408.
6. ^ Zimmermann K, Hoischen S, Hafner M, Nischt R (May 1995). “Genomic sequences and structural organization of the human nidogen gene (NID)”. Genomics. 27 (2): 245–50. doi:10.1006/geno.1995.1038. PMID7557988.
7. ^ Smith J, Ockleford CD (January 1994). “Laser scanning confocal examination and comparison of nidogen (entactin) with laminin in term human amniochorion”. Placenta. 15 (1):95–106. doi:10.1016/S0143-4004(05)80240-1. PMID8208674.
8. ^ Ockleford CD, Bright N, Hubbard A, D’Lacey C, Smith J, Gardiner L, Sheikh T, Albentosa M, Turtle K (October 1993). “Micro-Trabeculae, Macro-Plaques or Mini-Basement Membranes in Human Term Fetal Membranes?”. Phil. Trans. R. Soc. Lond. B. 342 (1300): 121–136. doi:10.1098/rstb.1993.0142. PMID7904354.
9. ^ Yurchenco PD, Patton BL (2009). “Developmental and pathogenic mechanisms of basement membrane assembly”. Curr. Pharm. Des. 15 (12): 1277–94. doi:10.2174/138161209787846766. PMC2978668. PMID19355968.
10. ^ “Entrez Gene: NID1 nidogen 1”.
11. ^ Yi XY, Wayner EA, Kim Y, Fish AJ (March 1998). “Adhesion of cultured human kidney mesangial cells to native entactin: role of integrin receptors”. Cell Adhes. Commun. 5 (3): 237–48. doi:10.3109/15419069809040294. PMID9686320.
12. ^ “OMIM Entry – % 609222 – DANDY-WALKER MALFORMATION WITH OCCIPITAL CEPHALOCELE, AUTOSOMAL DOMINANT; ADDWOC”. www.omim.org. Retrieved 2020-01-06.
13. ^ McNiven, Vanda; Ito, Yoko A.; Hartley, Taila; Kernohan, Kristin; Miller, Elka; Care4Rare Canada; Armour, Christine M. (May 2019). “NID1 variant associated with occipital cephaloceles in a family expressing a spectrum of phenotypes”. American Journal of Medical Genetics. Part A. 179 (5): 837–841. doi:10.1002/ajmg.a.61095. ISSN1552-4833. PMID30773799. S2CID73507129.
14. ^ Adam S, Göhring W, Wiedemann H, Chu ML, Timpl R, Kostka G (September 1997). “Binding of fibulin-1 to nidogen depends on its C-terminal globular domain and a specific array of calcium-binding epidermal growth factor-like (EG) modules“. J. Mol. Biol. 272 (2): 226–36. doi:10.1006/jmbi.1997.1244. PMID9299350.
15. ^Tran H, VanDusen WJ, Argraves WS (September 1997). “The self-association and fibronectin-binding sites of fibulin-1 map to calcium-binding epidermal growth factor-like domains”. J. Biol. Chem. 272 (36): 22600–6. doi:10.1074/jbc.272.36.22600. PMID9278415.
16. ^ Pan TC, Kluge M, Zhang RZ, Mayer U, Timpl R, Chu ML (August 1993). “Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement-membrane ligands”. Eur. J. Biochem. 215 (3): 733–40. doi:10.1111/j.1432-1033.1993.tb18086.x. PMID8354280.

Further reading[edit]

• Chung AE, Durkin ME (1990). “Entactin: structure and function”. Am. J. Respir. Cell Mol. Biol. 3 (4): 275–82. doi:10.1165/ajrcmb/3.4.275. PMID2119632.
• Yurchenco PD, Schittny JC (1990). “Molecular architecture of basement membranes”. FASEB J. 4 (6): 1577–90. doi:10.1096/fasebj.4.6.2180767. PMID2180767. S2CID18724722.

External links[edit]

• Nidogen at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
• Overview of all the structural information available in the PDB for UniProt: P10493 (Mouse Nidogen-1) at the PDBe-KB.

Laminin Domain I
Identifiers
Symbol	Laminin_I
Pfam	PF06008
InterPro	IPR009254

Available protein structures:

Laminin Domain II
Identifiers
Symbol	Laminin_II
Pfam	PF06009
InterPro	IPR010307

Available protein structures:

Laminin B (Domain IV)
Identifiers
Symbol	Laminin_B
Pfam	PF00052
InterPro	IPR000034

Available protein structures:

Laminin EGF-like (Domains III and V)
crystal structure of three consecutive laminin-type epidermal growth factor-like (le) modules of laminin gamma1 chain harboring the nidogen binding site
Identifiers
Symbol	Laminin_EGF
Pfam	PF00053
Pfam clan	CL0001
InterPro	IPR002049
PROSITE	PDOC00021
SCOP2	1tle / SCOPe / SUPFAM

Available protein structures:

Laminin G domain
laminin alpha 2 chain lg4-5 domain pair, ca1 site mutant
Identifiers
Symbol	Laminin_G_1
Pfam	PF00054
Pfam clan	CL0004
InterPro	IPR012679
SCOP2	1qu0 / SCOPe / SUPFAM

Available protein structures:

Laminin G domain
the structure of the ligand-binding domain of neurexin 1beta: regulation of lns domain function by alternative splicing
Identifiers
Symbol	Laminin_G_2
Pfam	PF02210
Pfam clan	CL0004
InterPro	IPR012680
SMART	TSPN

Available protein structures:

Laminin N-terminal (Domain VI)
Identifiers
Symbol	Laminin_N
Pfam	PF00055
Pfam clan	CL0202
InterPro	IPR008211
SMART	LamNT
SCOP2	1klo / SCOPe / SUPFAM

Available protein structures:

Laminins contain several conserved protein domains.

Laminin I and Laminin II

Laminins are trimeric molecules; laminin-1 is an alpha1 beta1 gamma1 trimer. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coilstructure.^[22]

Laminin B

The laminin B domain (also known as domain IV) is an extracellular module of unknown function. It is found in a number of different proteins that include, heparan sulphate proteoglycan from basement membrane, a laminin-like protein from Caenorhabditis elegans and laminin. Laminin IV domain is not found in short laminin chains (alpha4 or beta3).

Laminin EGF-like

Beside different types of globular domains each laminin subunit contains, in its first half, consecutive repeats of about 60 amino acids in length that include eight conserved cysteines.^[23] The tertiary structure of this domain is remotely similar in its N-terminus to that of the EGF-like module.^[24][25] It is also known as a ‘LE’ or ‘laminin-type EGF-like’ domain. The number of copies of the laminin EGF-like domain in the different forms of laminins is highly variable; from 3 up to 22 copies have been found. In mouse laminin gamma-1 chain, the seventh LE domain has been shown to be the only one that binds with a high affinity to nidogen.^[26] The binding-sites are located on the surface within the loops C1-C3 and C5-C6.^[24][25] Long consecutive arrays of laminin EGF-like domains in laminins form rod-like elements of limited flexibility, which determine the spacing in the formation of laminin networks of basement membranes.^[27][28]

https://en.wikipedia.org/wiki/N-terminus

The N-terminus (also known as the amino-terminus, NH₂-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide, referring to the free amine group (-NH₂) located at the end of a polypeptide. Within a peptide, the amine group is bonded to the carboxylic group of another amino acid, making it a chain. That leaves a free carboxylic group at one end of the peptide, called the C-terminus, and a free amine group on the other end called the N-terminus. By convention, peptide sequences are written N-terminus to C-terminus, left to right (in LTR writing systems).^[1] This correlates the translation direction to the text direction, because when a protein is translated from messenger RNA, it is created from the N-terminus to the C-terminus, as amino acids are added to the carboxyl end of the protein.

Laminin G

The laminin globular (G) domain, also known as the LNS (Laminin-alpha, Neurexin and Sex hormone-binding globulin) domain, is on average 177 amino acids in length and can be found in one to six copies in various laminin family members as well as in a large number of other extracellular proteins.^[29] For example, all laminin alpha-chains have five laminin G domains, all collagen family proteins have one laminin G domain, the CNTNAP proteins have four laminin G domains, while neurexin 1 and 2 each hold six laminin G domains. On average, approximately one quarter of the proteins that hold laminin G domains is taken up by these laminin G domains themselves. The smallest laminin G domain can be found in one of the collagen proteins (COL24A1; 77 AA) and the largest domain in TSPEAR (219 AA).

The exact function of the Laminin G domains has remained elusive, and a variety of binding functions has been ascribed to different Laminin G modules. For example, the laminin alpha1 and alpha2 chains each have five C-terminal laminin G domains, where only domains LG4 and LG5 contain binding sites for heparin, sulphatides and the cell surface receptor dystroglycan.^[30] Laminin G-containing proteins appear to have a wide variety of roles in cell adhesion, signalling, migration, assembly and differentiation.

Laminin N-terminal

Basement membrane assembly is a cooperative process in which laminins polymerise through their N-terminal domain (LN or domain VI) and anchor to the cell surface through their G domains. Netrins may also associate with this network through heterotypic LN domain interactions.^[28] This leads to cell signalling through integrins and dystroglycan (and possibly other receptors) recruited to the adherent laminin.This LN domain-dependent self-assembly is considered to be crucial for the integrity of basement membranes, as highlighted by genetic forms of muscular dystrophy containing the deletion of the LN module from the alpha 2 laminin chain.^[31] The laminin N-terminal domain is found in all laminin and netrin subunits except laminin alpha 3A, alpha 4 and gamma 2.

Human proteins containing laminin domains

• Laminin domain I: all laminin alpha chains (LAMA1, LAMA2, LAMA3, LAMA4, LAMA5)
• Laminin domain II: all laminin alpha chains (LAMA1, LAMA2, LAMA3, LAMA4, LAMA5)
• Laminin B (domain IV): all laminin alpha chains (LAMA1, LAMA2, LAMA3, LAMA4, LAMA5), gamma chains (LAMC1, LAMC2, LAMC3), and perlecan (HSPG2)
• Laminin EGF-like (domains III and V): all laminin chains (LAMA1, LAMA2, LAMA3, LAMA4, LAMA5, LAMB1, LAMB2, LAMB3, LAMB4, LAMC1, LAMC2, LAMC3), attractins (ATRN, ATRNL1), cadherin EGF LAG seven-pass G-type receptors (CELSR1, CELSR2, CELSR3), cysteine-rich with EGF-like domain proteins (CRELD1, CRELD2), multiple EGF-like domain proteins (MEGF6, MEGF8, MEGF9, MEGF10, PEAR1), most netrins (NTN1, NTN3, NTN4, NTNG1, NTNG2), mucins 3A and 3B (MUC3A, MUC3B), class F scavenger receptors (SCARF1, SCARF2), stabilins (STAB1, STAB2), agrin (AGRIN), angiopoietin-1 receptor (TEK), perlecan (HSPG2), tenascin N (TNN), and usherin (USH2A).
• Laminin G domain: all laminin alpha chains (LAMA1, LAMA2, LAMA3, LAMA4, LAMA5), cadherin EGF LAG seven-pass G-type receptors (CELSR1, CELSR2, CELSR3), contactin-associated proteins (CNTNAP1, CNTNAP2, CNTNAP3, CNTNAP3B, CNTNAP4, CNTNAP5), some collagens (COL5A1, COL5A3, COL9A1, COL11A1, COL11A2, COL12A1, COL14A1, COL15A1, COL16A1, COL18A1, COL19A1, COL20A1, COL21A1, COL22A1, COL24A1, COL27A1), crumbs homologs 1 and 2 (CRB1, CRB2), fat homologs (FAT1, FAT2, FAT3, FAT4), NEL-like proteins (NELL1, NELL2), neurexins (NRXN1, NRXN2, NRXN3), slit homologs (SLIT1, SLIT2, SLIT3), thrombospondins (THBS1, THBS2, THBS3, THBS4, TSPEAR), agrin (AGRIN), chondroitin sulfate proteoglycan 4 (CSPG4), eyes shut homolog (EYS), growth arrest-specific protein 6 (GAS6), perlecan (HSPG2), pikachurin (EGFLAM), protein S (PROS1), sex hormone-binding globulin (SHBG) and usherin (USH2A)
• Laminin N-terminal (domain VI): most laminin chains (LAMA1, LAMA2, LAMA3, LAMA5, LAMB1, LAMB2, LAMB3, LAMB4, LAMC1, LAMC3), most netrins (NTN1, NTN3, NTN4, NTNG1, NTNG2), and usherin (USH2A)

See also

• Substrate adhesion molecules
• Laminin database
• List of target antigens in pemphigoid

References

1.  Timpl R, Rohde H, Robey PG, Rennard SI, Foidart JM, Martin GR (October 1979). “Laminin–a glycoprotein from basement membranes”. The Journal of Biological Chemistry. 254 (19): 9933–7. doi:10.1016/S0021-9258(19)83607-4. PMID114518.

  Durbeej, Madeleine (January 2010). “Laminins”. Cell and Tissue Research. 339 (1): 259–268. doi:10.1007/s00441-009-0838-2. ISSN1432-0878. PMID19693542 – via Springer Link.

  Aumailley M, Bruckner-Tuderman L, Carter WG, Deutzmann R, Edgar D, Ekblom P, Engel J, Engvall E, Hohenester E, Jones JC, Kleinman HK, Marinkovich MP, Martin GR, Mayer U, Meneguzzi G, Miner JH, Miyazaki K, Patarroyo M, Paulsson M, Quaranta V, Sanes JR, Sasaki T, Sekiguchi K, Sorokin LM, Talts JF, Tryggvason K, Uitto J, Virtanen I, von der Mark K, Wewer UM, Yamada Y, Yurchenco PD (August 2005). “A simplified laminin nomenclature”. Matrix Biology. 24 (5): 326–32. doi:10.1016/j.matbio.2005.05.006. PMID15979864.

  M. A. Haralson; John R. Hassell (1995). Extracellular matrix: a practical approach. Ithaca, N.Y: IRL Press. ISBN978-0-19-963220-6.

  Yurchenco PD, Patton BL (2009). “Developmental and pathogenic mechanisms of basement membrane assembly”. Current Pharmaceutical Design. 15 (12): 1277–94.doi:10.2174/138161209787846766. PMC2978668. PMID19355968.

  Colognato H, Yurchenco PD (June 2000). “Form and function: the laminin family of heterotrimers”. Developmental Dynamics. 218 (2): 213–34. doi:10.1002/(SICI)1097-0177(200006)218:2<213::AID-DVDY1>3.0.CO;2-R. PMID10842354.

  Royce, Peter M., ed. (2002). Connective tissue and its heritable disorders: molecular, genetic, and medical aspects (2nd ed.). New York: Wiley-Liss. p. 306. ISBN9780471251859.

  Kühn, Klaus (1997). “Extracellular matrix constituents as integrin ligands”. In Elbe, Johannes A. (ed.). Integrin-ligand interaction. New York: Chapman & Hall. p. 50. ISBN9780412138614.

  Smith J, Ockleford CD (January 1994). “Laser scanning confocal examination and comparison of nidogen (entactin) with laminin in term human amniochorion”. Placenta. 15 (1): 95–106. doi:10.1016/S0143-4004(05)80240-1. PMID8208674.

  Ockleford C, Bright N, Hubbard A, D’Lacey C, Smith J, Gardiner L, Sheikh T, Albentosa M, Turtle K (October 1993). “Micro-trabeculae, macro-plaques or mini-basement membranes in human term fetal membranes?”. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 342 (1300): 121–36. doi:10.1098/rstb.1993.0142. PMID7904354.

  Beck et al., 1999.^[specify]

  Ichikawa N, Kasai S, Suzuki N, Nishi N, Oishi S, Fujii N, Kadoya Y, Hatori K, Mizuno Y, Nomizu M, Arikawa-Hirasawa E (April 2005). “Identification of neurite outgrowth active sites on the laminin alpha4 chain G domain”. Biochemistry.44 (15): 5755–62. doi:10.1021/bi0476228. PMID15823034.

  Beckmann G, Hanke J, Bork P, Reich JG (February 1998). “Merging extracellular domains: fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins”. Journal of Molecular Biology. 275 (5): 725–30. doi:10.1006/jmbi.1997.1510. PMID9480764.

  Nieuwenhuis, B.; Haenzi, B.; Andrews, M. R.; Verhaagen, J.; Fawcett, J. W. (2018). “Integrins promote axonal regeneration after injury of the nervous system”. Biological Reviews. 93 (3): 1339–1362. doi:10.1111/brv.12398. PMC6055631. PMID29446228.

  Hall TE, Bryson-Richardson RJ, Berger S, Jacoby AS, Cole NJ, Hollway GE, Berger J, Currie PD (April 2007). “The zebrafish candyfloss mutant implicates extracellular matrix adhesion failure in laminin alpha2-deficient congenital muscular dystrophy”. Proceedings of the National Academy of Sciences of the United States of America. 104 (17): 7092–7. Bibcode:2007PNAS..104.7092H. doi:10.1073/pnas.0700942104. PMC1855385. PMID17438294.

  Petz M, Them N, Huber H, Beug H, Mikulits W (January 2012). “La enhances IRES-mediated translation of laminin B1 during malignant epithelial to mesenchymal transition”. Nucleic Acids Research. 40 (1): 290–302. doi:10.1093/nar/gkr717. PMC3245933. PMID21896617.

  Wondimu Z, Gorfu G, Kawataki T, Smirnov S, Yurchenco P, Tryggvason K, Patarroyo M (March 2006). “Characterization of commercial laminin preparations from human placenta in comparison to recombinant laminins 2 (alpha2beta1gamma1), 8 (alpha4beta1gamma1), 10 (alpha5beta1gamma1)”. Matrix Biology. 25 (2): 89–93. doi:10.1016/j.matbio.2005.10.001. PMID16289578.

  Kortesmaa, Jarkko; Yurchenco, Peter; Tryggvason, Karl (19 May 2000). “Recombinant Laminin-8 (α4β1γ1)”. Journal of Biological Chemistry. 275 (20): 14853–14859. doi:10.1074/jbc.275.20.14853. PMID10809728.

  Domogatskaya A, Rodin S, Boutaud A, Tryggvason K (November 2008). “Laminin-511 but not -332, -111, or -411 enables mouse embryonic stem cell self-renewal in vitro”. Stem Cells. 26 (11): 2800–9. doi:10.1634/stemcells.2007-0389. PMID 18757303.

  Miyazaki T, Futaki S, Hasegawa K, Kawasaki M, Sanzen N, Hayashi M, Kawase E, Sekiguchi K, Nakatsuji N, Suemori H (October 2008). “Recombinant human laminin isoforms can support the undifferentiated growth of human embryonic stem cells”. Biochemical and Biophysical Research Communications. 375 (1): 27–32. doi:10.1016/j.bbrc.2008.07.111. PMID18675790.

  Rodin S, Domogatskaya A, Ström S, Hansson EM, Chien KR, Inzunza J, Hovatta O, Tryggvason K (June 2010). “Long-term self-renewal of human pluripotent stem cells on human recombinant laminin-511”. Nature Biotechnology. 28 (6): 611–5. doi:10.1038/nbt.1620. hdl:10616/40259. PMID20512123. S2CID10801152.

  Sasaki M, Kleinman HK, Huber H, Deutzmann R, Yamada Y (November 1988). “Laminin, a multidomain protein. The A chain has a unique globular domain and homology with the basement membrane proteoglycan and the laminin B chains”. The Journal of Biological Chemistry. 263 (32): 16536–44. doi:10.1016/S0021-9258(18)37424-6. PMID3182802.

  Engel J (July 1989). “EGF-like domains in extracellular matrix proteins: localized signals for growth and differentiation?”. FEBS Letters. 251 (1–2): 1–7. doi:10.1016/0014-5793(89)81417-6. PMID2666164. S2CID36607427.

  Stetefeld J, Mayer U, Timpl R, Huber R (April 1996). “Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin gamma1 chain harboring the nidogen binding site“. Journal of Molecular Biology. 257 (3): 644–57. doi:10.1006/jmbi.1996.0191. PMID8648630.

  Baumgartner R, Czisch M, Mayer U, Pöschl E, Huber R, Timpl R, Holak TA (April 1996). “Structure of the nidogen binding LE module of the laminin gamma1 chain in solution”. Journal of Molecular Biology. 257 (3): 658–68. doi:10.1006/jmbi.1996.0192. PMID8648631.

  Mayer U, Pöschl E, Gerecke DR, Wagman DW, Burgeson RE, Timpl R (May 1995). “Low nidogen affinity of laminin-5 can be attributed to two serine residues in EGF-like motif gamma 2III4”. FEBS Letters. 365 (2–3): 129–32. doi:10.1016/0014-5793(95)00438-F. PMID7781764. S2CID21559588.

  Beck K, Hunter I, Engel J (February 1990). “Structure and function of laminin: anatomy of a multidomain glycoprotein”. FASEB Journal. 4 (2): 148–60. doi:10.1096/fasebj.4.2.2404817. PMID2404817.

  Yurchenco PD, Cheng YS (August 1993). “Self-assembly and calcium-binding sites in laminin. A three-arm interaction model”. The Journal of Biological Chemistry. 268 (23): 17286–99. doi:10.1016/S0021-9258(19)85334-6. PMID8349613.

  “Laminin G domain”. InterPro. European Bioinformatics Institute. Retrieved 22 February 2016.

  Tisi D, Talts JF, Timpl R, Hohenester E (April 2000). “Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for alpha-dystroglycan and heparin”. The EMBO Journal. 19 (7): 1432–40. doi:10.1093/emboj/19.7.1432. PMC310212. PMID10747011.

1.  Xu H, Wu XR, Wewer UM, Engvall E (November 1994). “Murine muscular dystrophy caused by a mutation in the laminin alpha 2 (Lama2) gene”. Nature Genetics. 8 (3): 297–302. doi:10.1038/ng1194-297. PMID7874173. S2CID21549628.