Laminin, gamma 1: Difference between revisions

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{{Infobox_gene}}
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'''Laminin subunit gamma-1''' is a [[protein]] that in humans is encoded by the ''LAMC1'' [[gene]].<ref name="pmid3234037">{{cite journal |vauthors=Fukushima Y, Pikkarainen T, Kallunki T, Eddy RL, Byers MG, Haley LL, Henry WM, Tryggvason K, Shows TB | title = Isolation of a human laminin B2 (LAMB2) cDNA clone and assignment of the gene to chromosome region 1q25----q31 | journal = Cytogenet Cell Genet | volume = 48 | issue = 3 | pages = 137–41 |date=May 1989 | pmid = 3234037 | pmc =  | doi =10.1159/000132610 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: LAMC1 laminin, gamma 1 (formerly LAMB2)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3915| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_LAMC1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1klo.
| PDB = {{PDB2|1klo}}, {{PDB2|1npe}}, {{PDB2|1tle}}
| Name = Laminin, gamma 1 (formerly LAMB2)
| HGNCid = 6492
| Symbol = LAMC1
| AltSymbols =; LAMB2; MGC87297
| OMIM = 150290
| ECnumber =
| Homologene = 1724
| MGIid = 99914
| GeneAtlas_image1 = PBB_GE_LAMC1_200771_at_tn.png
  | GeneAtlas_image2 = PBB_GE_LAMC1_200770_s_at_tn.png
  | Function = {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005604 |text = basement membrane}} {{GNF_GO|id=GO:0005606 |text = laminin-1 complex}}
| Process = {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007492 |text = endoderm development}} {{GNF_GO|id=GO:0050679 |text = positive regulation of epithelial cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3915
    | Hs_Ensembl = ENSG00000135862
    | Hs_RefseqProtein = NP_002284
    | Hs_RefseqmRNA = NM_002293
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 181259176
    | Hs_GenLoc_end = 181381350
    | Hs_Uniprot = P11047
    | Mm_EntrezGene = 226519
    | Mm_Ensembl = ENSMUSG00000026478
    | Mm_RefseqmRNA = NM_010683
    | Mm_RefseqProtein = NP_034813
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 154981138
    | Mm_GenLoc_end = 155095004
    | Mm_Uniprot = Q3TRH4
  }}
}}
'''Laminin, gamma 1 (formerly LAMB2)''', also known as '''LAMC1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LAMC1 laminin, gamma 1 (formerly LAMB2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3915| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the gamma chain isoform laminin, gamma 1. The gamma 1 chain, formerly thought to be a beta chain, contains structural domains similar to beta chains, however, lacks the short alpha region separating domains I and II. The structural organization of this gene also suggested that it had diverged considerably from the beta chain genes. Embryos of transgenic mice in which both alleles of the gamma 1 chain gene were inactivated by homologous recombination, lacked basement membranes, indicating that laminin, gamma 1 chain is necessary for laminin heterotrimer assembly. It has been inferred by analogy with the strikingly similar 3' UTR sequence in mouse laminin gamma 1 cDNA, that multiple polyadenylation sites are utilized in human to generate the 2 different sized mRNAs (5.5 and 7.5 kb) seen on Northern analysis.<ref name="entrez">{{cite web | title = Entrez Gene: LAMC1 laminin, gamma 1 (formerly LAMB2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3915| accessdate = }}</ref>
| summary_text = [[Laminin]]s, a family of extracellular matrix [[glycoprotein]]s, are the major noncollagenous constituent of [[basement membrane]]s. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct [[gene]]. Several [[Protein isoform|isoforms]] of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the gamma chain isoform laminin, gamma 1. The gamma 1 chain, formerly thought to be a beta chain, contains structural domains similar to beta chains, however, lacks the short alpha region separating domains I and II. The structural organization of this gene also suggested that it had diverged considerably from the beta chain genes. Embryos of transgenic mice in which both alleles of the gamma 1 chain gene were inactivated by homologous recombination, lacked basement membranes, indicating that laminin, gamma 1 chain is necessary for laminin heterotrimer assembly. It has been inferred by analogy with the strikingly similar 3' UTR sequence in mouse laminin gamma 1 [[cDNA]], that multiple polyadenylation sites are utilized in human to generate the 2 different sized mRNAs (5.5 and 7.5 kb) seen on Northern analysis.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Ljubimova JY, Fujita M, Khazenzon NM, ''et al.'' |title=Changes in laminin isoforms associated with brain tumor invasion and angiogenesis. |journal=Front. Biosci. |volume=11 |issue=  |pages= 81-8 |year= 2006 |pmid= 16146715 |doi= }}
*{{cite journal   |vauthors=Ljubimova JY, Fujita M, Khazenzon NM, etal |title=Changes in laminin isoforms associated with brain tumor invasion and angiogenesis. |journal=Front. Biosci. |volume=11 |issue=  1|pages= 81–8 |year= 2006 |pmid= 16146715 |doi=10.2741/1781 |pmc=3506377}}
*{{cite journal  | author=Santos CL, Sabbaga J, Brentani R |title=Differences in human laminin B2 sequences. |journal=DNA Seq. |volume=1 |issue= 4 |pages= 275-7 |year= 1992 |pmid= 1806043 |doi=  }}
*{{cite journal  |vauthors=Santos CL, Sabbaga J, Brentani R |title=Differences in human laminin B2 sequences. |journal=DNA Seq. |volume=1 |issue= 4 |pages= 275–7 |year= 1992 |pmid= 1806043 |doi=10.3109/10425179109020782 }}
*{{cite journal | author=Kallunki T, Ikonen J, Chow LT, ''et al.'' |title=Structure of the human laminin B2 chain gene reveals extensive divergence from the laminin B1 chain gene. |journal=J. Biol. Chem. |volume=266 |issue= 1 |pages= 221-8 |year= 1991 |pmid= 1985895 |doi=  }}
*{{cite journal   |vauthors=Kallunki T, Ikonen J, Chow LT, etal |title=Structure of the human laminin B2 chain gene reveals extensive divergence from the laminin B1 chain gene. |journal=J. Biol. Chem. |volume=266 |issue= 1 |pages= 221–8 |year= 1991 |pmid= 1985895 |doi=  }}
*{{cite journal  | author=Hunter DD, Shah V, Merlie JP, Sanes JR |title=A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction. |journal=Nature |volume=338 |issue= 6212 |pages= 229-34 |year= 1989 |pmid= 2922051 |doi= 10.1038/338229a0 }}
*{{cite journal  |vauthors=Hunter DD, Shah V, Merlie JP, Sanes JR |title=A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction. |journal=Nature |volume=338 |issue= 6212 |pages= 229–34 |year= 1989 |pmid= 2922051 |doi= 10.1038/338229a0 }}
*{{cite journal  | author=Fukushima Y, Pikkarainen T, Kallunki T, ''et al.'' |title=Isolation of a human laminin B2 (LAMB2) cDNA clone and assignment of the gene to chromosome region 1q25----q31. |journal=Cytogenet. Cell Genet. |volume=48 |issue= 3 |pages= 137-41 |year= 1989 |pmid= 3234037 |doi=  }}
*{{cite journal  |vauthors=Pikkarainen T, Kallunki T, Tryggvason K |title=Human laminin B2 chain. Comparison of the complete amino acid sequence with the B1 chain reveals variability in sequence homology between different structural domains. |journal=J. Biol. Chem. |volume=263 |issue= 14 |pages= 6751–8 |year= 1988 |pmid= 3360804 |doi=  }}
*{{cite journal | author=Pikkarainen T, Kallunki T, Tryggvason K |title=Human laminin B2 chain. Comparison of the complete amino acid sequence with the B1 chain reveals variability in sequence homology between different structural domains. |journal=J. Biol. Chem. |volume=263 |issue= 14 |pages= 6751-8 |year= 1988 |pmid= 3360804 |doi=  }}
*{{cite journal   |vauthors=Mattei MG, Weil D, Pribula-Conway D, etal |title=cDNA cloning, expression and mapping of human laminin B2 gene to chromosome 1q31. |journal=Hum. Genet. |volume=79 |issue= 3 |pages= 235–41 |year= 1988 |pmid= 3402995 |doi=10.1007/BF00366243 }}
*{{cite journal  | author=Mattei MG, Weil D, Pribula-Conway D, ''et al.'' |title=cDNA cloning, expression and mapping of human laminin B2 gene to chromosome 1q31. |journal=Hum. Genet. |volume=79 |issue= 3 |pages= 235-41 |year= 1988 |pmid= 3402995 |doi=  }}
*{{cite journal  |vauthors=Davis JM, Narachi MA, Alton NK, Arakawa T |title=Structure of human tumor necrosis factor alpha derived from recombinant DNA. |journal=Biochemistry |volume=26 |issue= 5 |pages= 1322–6 |year= 1987 |pmid= 3552045 |doi=10.1021/bi00379a018 }}
*{{cite journal | author=Davis JM, Narachi MA, Alton NK, Arakawa T |title=Structure of human tumor necrosis factor alpha derived from recombinant DNA. |journal=Biochemistry |volume=26 |issue= 5 |pages= 1322-6 |year= 1987 |pmid= 3552045 |doi= }}
*{{cite journal   |vauthors=Wewer UM, Gerecke DR, Durkin ME, etal |title=Human beta 2 chain of laminin (formerly S chain): cDNA cloning, chromosomal localization, and expression in carcinomas. |journal=Genomics |volume=24 |issue= 2 |pages= 243–52 |year= 1995 |pmid= 7698745 |doi= 10.1006/geno.1994.1612 }}
*{{cite journal | author=Wewer UM, Gerecke DR, Durkin ME, ''et al.'' |title=Human beta 2 chain of laminin (formerly S chain): cDNA cloning, chromosomal localization, and expression in carcinomas. |journal=Genomics |volume=24 |issue= 2 |pages= 243-52 |year= 1995 |pmid= 7698745 |doi= 10.1006/geno.1994.1612 }}
*{{cite journal   |vauthors=Burgeson RE, Chiquet M, Deutzmann R, etal |title=A new nomenclature for the laminins. |journal=Matrix Biol. |volume=14 |issue= 3 |pages= 209–11 |year= 1994 |pmid= 7921537 |doi=10.1016/0945-053X(94)90184-8  }}
*{{cite journal  | author=Burgeson RE, Chiquet M, Deutzmann R, ''et al.'' |title=A new nomenclature for the laminins. |journal=Matrix Biol. |volume=14 |issue= 3 |pages= 209-11 |year= 1994 |pmid= 7921537 |doi=  }}
*{{cite journal  |vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }}
*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi=  }}
*{{cite journal  |vauthors=O'Grady P, Thai TC, Saito H |title=The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR. |journal=J. Cell Biol. |volume=141 |issue= 7 |pages= 1675–84 |year= 1998 |pmid= 9647658 |doi=10.1083/jcb.141.7.1675  | pmc=2133008 }}
*{{cite journal  | author=O'Grady P, Thai TC, Saito H |title=The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR. |journal=J. Cell Biol. |volume=141 |issue= 7 |pages= 1675-84 |year= 1998 |pmid= 9647658 |doi= }}
*{{cite journal  |vauthors=Kohfeldt E, Sasaki T, Göhring W, Timpl R |title=Nidogen-2: a new basement membrane protein with diverse binding properties. |journal=J. Mol. Biol. |volume=282 |issue= 1 |pages= 99–109 |year= 1998 |pmid= 9733643 |doi= 10.1006/jmbi.1998.2004 }}
*{{cite journal | author=Kohfeldt E, Sasaki T, Göhring W, Timpl R |title=Nidogen-2: a new basement membrane protein with diverse binding properties. |journal=J. Mol. Biol. |volume=282 |issue= 1 |pages= 99-109 |year= 1998 |pmid= 9733643 |doi= 10.1006/jmbi.1998.2004 }}
*{{cite journal   |vauthors=Suzuki H, Denisenko ON, Suzuki Y, etal |title=Inducible transcriptional activity of bcn-1 element from laminin gamma1-chain gene promoter in renal and nonrenal cells. |journal=Am. J. Physiol. |volume=275 |issue= 4 Pt 2 |pages= F518–26 |year= 1998 |pmid= 9755123 |doi= }}
*{{cite journal | author=Suzuki H, Denisenko ON, Suzuki Y, ''et al.'' |title=Inducible transcriptional activity of bcn-1 element from laminin gamma1-chain gene promoter in renal and nonrenal cells. |journal=Am. J. Physiol. |volume=275 |issue= 4 Pt 2 |pages= F518-26 |year= 1998 |pmid= 9755123 |doi= }}
*{{cite journal   |vauthors=Smyth N, Vatansever HS, Murray P, etal |title=Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation. |journal=J. Cell Biol. |volume=144 |issue= 1 |pages= 151–60 |year= 1999 |pmid= 9885251 |doi=10.1083/jcb.144.1.151  | pmc=2148127  }}
*{{cite journal | author=Smyth N, Vatansever HS, Murray P, ''et al.'' |title=Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation. |journal=J. Cell Biol. |volume=144 |issue= 1 |pages= 151-60 |year= 1999 |pmid= 9885251 |doi=  }}
*{{cite journal   |vauthors=Kikkawa Y, Sanzen N, Fujiwara H, etal |title=Integrin binding specificity of laminin-10/11: laminin-10/11 are recognized by alpha 3 beta 1, alpha 6 beta 1 and alpha 6 beta 4 integrins.  | series=113 |journal=J. Cell Sci. |volume=( Pt 5) |issue= |pages= 869–76 |year= 2000 |pmid= 10671376 |doi=  }}
*{{cite journal | author=Kikkawa Y, Sanzen N, Fujiwara H, ''et al.'' |title=Integrin binding specificity of laminin-10/11: laminin-10/11 are recognized by alpha 3 beta 1, alpha 6 beta 1 and alpha 6 beta 4 integrins. |journal=J. Cell. Sci. |volume=113 ( Pt 5) |issue= |pages= 869-76 |year= 2000 |pmid= 10671376 |doi= }}
*{{cite journal   |vauthors=Champliaud MF, Virtanen I, Tiger CF, etal |title=Posttranslational modifications and beta/gamma chain associations of human laminin alpha1 and laminin alpha5 chains: purification of laminin-3 from placenta. |journal=Exp. Cell Res. |volume=259 |issue= 2 |pages= 326–35 |year= 2000 |pmid= 10964500 |doi= 10.1006/excr.2000.4980 }}
*{{cite journal | author=Champliaud MF, Virtanen I, Tiger CF, ''et al.'' |title=Posttranslational modifications and beta/gamma chain associations of human laminin alpha1 and laminin alpha5 chains: purification of laminin-3 from placenta. |journal=Exp. Cell Res. |volume=259 |issue= 2 |pages= 326-35 |year= 2000 |pmid= 10964500 |doi= 10.1006/excr.2000.4980 }}
*{{cite journal   |vauthors=Pedraza C, Geberhiwot T, Ingerpuu S, etal |title=Monocytic cells synthesize, adhere to, and migrate on laminin-8 (alpha 4 beta 1 gamma 1). |journal=J. Immunol. |volume=165 |issue= 10 |pages= 5831–8 |year= 2000 |pmid= 11067943 |doi= 10.4049/jimmunol.165.10.5831}}
*{{cite journal | author=Pedraza C, Geberhiwot T, Ingerpuu S, ''et al.'' |title=Monocytic cells synthesize, adhere to, and migrate on laminin-8 (alpha 4 beta 1 gamma 1). |journal=J. Immunol. |volume=165 |issue= 10 |pages= 5831-8 |year= 2000 |pmid= 11067943 |doi=  }}
*{{cite journal   |vauthors=Parsons SF, Lee G, Spring FA, etal |title=Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity. |journal=Blood |volume=97 |issue= 1 |pages= 312–20 |year= 2001 |pmid= 11133776 |doi=10.1182/blood.V97.1.312 }}
*{{cite journal  | author=Parsons SF, Lee G, Spring FA, ''et al.'' |title=Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity. |journal=Blood |volume=97 |issue= 1 |pages= 312-20 |year= 2001 |pmid= 11133776 |doi= }}
*{{cite journal  |vauthors=McArthur CP, Wang Y, Heruth D, Gustafson S |title=Amplification of extracellular matrix and oncogenes in tat-transfected human salivary gland cell lines with expression of laminin, fibronectin, collagens I, III, IV, c-myc and p53. |journal=Arch. Oral Biol. |volume=46 |issue= 6 |pages= 545–55 |year= 2001 |pmid= 11311202 |doi=10.1016/S0003-9969(01)00014-0 }}
*{{cite journal  | author=McArthur CP, Wang Y, Heruth D, Gustafson S |title=Amplification of extracellular matrix and oncogenes in tat-transfected human salivary gland cell lines with expression of laminin, fibronectin, collagens I, III, IV, c-myc and p53. |journal=Arch. Oral Biol. |volume=46 |issue= 6 |pages= 545-55 |year= 2001 |pmid= 11311202 |doi= }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=3915}}
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{{Fibrous proteins}}


{{protein-stub}}
[[Category:Laminins]]
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Latest revision as of 20:15, 8 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
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View/Edit Human

Laminin subunit gamma-1 is a protein that in humans is encoded by the LAMC1 gene.[1][2]

Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the gamma chain isoform laminin, gamma 1. The gamma 1 chain, formerly thought to be a beta chain, contains structural domains similar to beta chains, however, lacks the short alpha region separating domains I and II. The structural organization of this gene also suggested that it had diverged considerably from the beta chain genes. Embryos of transgenic mice in which both alleles of the gamma 1 chain gene were inactivated by homologous recombination, lacked basement membranes, indicating that laminin, gamma 1 chain is necessary for laminin heterotrimer assembly. It has been inferred by analogy with the strikingly similar 3' UTR sequence in mouse laminin gamma 1 cDNA, that multiple polyadenylation sites are utilized in human to generate the 2 different sized mRNAs (5.5 and 7.5 kb) seen on Northern analysis.[2]

References

  1. ↑ Fukushima Y, Pikkarainen T, Kallunki T, Eddy RL, Byers MG, Haley LL, Henry WM, Tryggvason K, Shows TB (May 1989). "Isolation of a human laminin B2 (LAMB2) cDNA clone and assignment of the gene to chromosome region 1q25----q31". Cytogenet Cell Genet. 48 (3): 137–41. doi:10.1159/000132610. PMID 3234037.
  2. ↑ 2.0 2.1 "Entrez Gene: LAMC1 laminin, gamma 1 (formerly LAMB2)".

Further reading


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