Ribosomal protein SA: Difference between revisions
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== Function == |
== Function == |
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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. Many of the effects of laminin are mediated through interactions with cell surface receptors. These receptors include members of the integrin family, as well as non-integrin laminin-binding proteins. The RPSA gene encodes a high-affinity, non-integrin family, laminin receptor 1. This receptor has been variously called 67 kD laminin receptor, 37 kD laminin receptor precursor (37LRP) and p40 ribosome-associated protein. The amino acid sequence of laminin receptor 1 is highly conserved through evolution, suggesting a key biological function. It has been observed that the level of the laminin receptor transcript is higher in colon carcinoma tissue and lung cancer cell |
[[Laminins]], a family of [[extracellular matrix]] [[glycoproteins]], are the major [[Collagen|noncollagenous]] constituent of [[basement membranes]]. They have been implicated in a wide variety of biological processes including [[cell adhesion]], [[Cellular_differentiation|differentiation]], [[Cell_migration|migration]], [[Cell_signaling|signaling]], [[neurite]] outgrowth and [[metastasis]]. Many of the effects of laminin are mediated through [[List_of_protein_interactions|interactions]] with [[cell surface receptors]]. These receptors include members of the [[integrin]] family, as well as non-integrin laminin-binding proteins. The RPSA gene encodes a high-affinity, non-integrin family, laminin receptor 1. This receptor has been variously called 67 kD laminin receptor, 37 kD laminin receptor precursor (37LRP) and p40 ribosome-associated protein. The [[amino acid]] [[Peptide_sequence|sequence]] of laminin receptor 1 is highly conserved through [[Evolutionary_biology|evolution]], suggesting a key [[biological function]]. It has been observed that the level of the laminin receptor [[Transcription_(genetics)|transcript]] is higher in [[colon]] [[carcinoma]] [[Tissue_(biology)|tissue]] and lung cancer cell lines than their normal counterparts. Also, there is a correlation between the [[Downregulation_and_upregulation|upregulation]] of this [[peptide|polypeptide]] in cancer cells and their invasive and metastatic [[phenotype]]. Multiple copies of this gene exist; however, most of them are [[pseudogene]]s thought to have arisen from [[Retroposon|retropositional]] events. Two [[Alternative_splicing|alternatively spliced]] transcript variants encoding the same protein have been found for this gene.<ref name="entrez"/> |
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== Interactions == |
== Interactions == |
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Revision as of 13:24, 25 February 2015
Template:PBB 40S ribosomal protein SA is a Ribosomal protein that in humans is encoded by the [[''RPSA'']] gene.[1][2][3]
Function
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. Many of the effects of laminin are mediated through interactions with cell surface receptors. These receptors include members of the integrin family, as well as non-integrin laminin-binding proteins. The RPSA gene encodes a high-affinity, non-integrin family, laminin receptor 1. This receptor has been variously called 67 kD laminin receptor, 37 kD laminin receptor precursor (37LRP) and p40 ribosome-associated protein. The amino acid sequence of laminin receptor 1 is highly conserved through evolution, suggesting a key biological function. It has been observed that the level of the laminin receptor transcript is higher in colon carcinoma tissue and lung cancer cell lines than their normal counterparts. Also, there is a correlation between the upregulation of this polypeptide in cancer cells and their invasive and metastatic phenotype. Multiple copies of this gene exist; however, most of them are pseudogenes thought to have arisen from retropositional events. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.[3]
Interactions
Ribosomal protein SA has been shown to interact with RPS21.[4][5]
References
- ^ Satoh K, Narumi K, Sakai T, Abe T, Kikuchi T, Matsushima K, Sindoh S, Motomiya M (Jul 1992). "Cloning of 67-kDa laminin receptor cDNA and gene expression in normal and malignant cell lines of the human lung". Cancer Lett. 62 (3): 199–203. doi:10.1016/0304-3835(92)90096-E. PMID 1534510.
- ^ Jackers P, Minoletti F, Belotti D, Clausse N, Sozzi G, Sobel ME, Castronovo V (Sep 1996). "Isolation from a multigene family of the active human gene of the metastasis-associated multifunctional protein 37LRP/p40 at chromosome 3p21.3". Oncogene. 13 (3): 495–503. PMID 8760291.
- ^ a b "Entrez Gene: RPSA ribosomal protein SA".
- ^ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–968. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
- ^ Sato M, Saeki Y, Tanaka K, Kaneda Y (Mar 1999). "Ribosome-associated protein LBP/p40 binds to S21 protein of 40S ribosome: analysis using a yeast two-hybrid system". Biochem. Biophys. Res. Commun. 256 (2): 385–390. doi:10.1006/bbrc.1999.0343. PMID 10079194.
Further reading
- Belkin AM, Stepp MA (2000). "Integrins as receptors for laminins". Microsc. Res. Tech. 51 (3): 280–301. doi:10.1002/1097-0029(20001101)51:3<280::AID-JEMT7>3.0.CO;2-O. PMID 11054877.
- Wewer UM, Liotta LA, Jaye M, Ricca GA, Drohan WN, Claysmith AP, Rao CN, Wirth P, Coligan JE, Albrechtsen R (1986). "Altered levels of laminin receptor mRNA in various human carcinoma cells that have different abilities to bind laminin". Proc. Natl. Acad. Sci. U.S.A. 83 (19): 7137–7141. doi:10.1073/pnas.83.19.7137. PMC 386670. PMID 2429301.
- Van den Ouweland AM, Van Duijnhoven HL, Deichmann KA, Van Groningen JJ, de Leij L, Van de Ven WJ (1989). "Characteristics of a multicopy gene family predominantly consisting of processed pseudogenes". Nucleic Acids Res. 17 (10): 3829–3843. doi:10.1093/nar/17.10.3829. PMC 317862. PMID 2543954.
- Yow HK, Wong JM, Chen HS, Lee CG, Davis S, Steele GD, Chen LB (1988). "Increased mRNA expression of a laminin-binding protein in human colon carcinoma: complete sequence of a full-length cDNA encoding the protein". Proc. Natl. Acad. Sci. U.S.A. 85 (17): 6394–6398. doi:10.1073/pnas.85.17.6394. PMC 281978. PMID 2970639.
- Gehlsen KR, Dillner L, Engvall E, Ruoslahti E (1988). "The human laminin receptor is a member of the integrin family of cell adhesion receptors". Science. 241 (4870): 1228–1229. doi:10.1126/science.2970671. PMID 2970671.
- Selvamurugan N, Eliceiri GL (1996). "The gene for human E2 small nucleolar RNA resides in an intron of a laminin-binding protein gene". Genomics. 30 (2): 400–1. PMID 8586453.
- Vladimirov SN, Ivanov AV, Karpova GG, Musolyamov AK, Egorov TA, Thiede B, Wittmann-Liebold B, Otto A (1996). "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry". Eur. J. Biochem. 239 (1): 144–149. doi:10.1111/j.1432-1033.1996.0144u.x. PMID 8706699.
- Clausse N, Jackers P, Jarès P, Joris B, Sobel ME, Castronovo V (1997). "Identification of the active gene coding for the metastasis-associated 37LRP/p40 multifunctional protein". DNA Cell Biol. 15 (12): 1009–1023. doi:10.1089/dna.1996.15.1009. PMID 8985115.
- Daidone MG, Silvestrini R, Benini E, Grigioni WF, D'Errico A (1997). "Expression of high-affinity 67-kDa laminin receptors in primary breast cancers and metachronous metastatic lesions or contralateral cancers". Br. J. Cancer. 76 (1): 52–3. doi:10.1038/bjc.1997.335. PMC 2223804. PMID 9218732.
- Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, Tanaka T, Page DC (1998). "A map of 75 human ribosomal protein genes". Genome Res. 8 (5): 509–23. doi:10.1101/gr.8.5.509. PMID 9582194.
- de Manzoni G, Guglielmi A, Verlato G, Tomezzoli A, Pelosi G, Schiavon I, Cordiano C (1998). "Prognostic significance of 67-kDa laminin receptor expression in advanced gastric cancer". Oncology. 55 (5): 456–460. doi:10.1159/000011895. PMID 9732225.
- Sato M, Saeki Y, Tanaka K, Kaneda Y (1999). "Ribosome-associated protein LBP/p40 binds to S21 protein of 40S ribosome: analysis using a yeast two-hybrid system". Biochem. Biophys. Res. Commun. 256 (2): 385–390. doi:10.1006/bbrc.1999.0343. PMID 10079194.
- Canfield SM, Khakoo AY (1999). "The nonintegrin laminin binding protein (p67 LBP) is expressed on a subset of activated human T lymphocytes and, together with the integrin very late activation antigen-6, mediates avid cellular adherence to laminin". J. Immunol. 163 (6): 3430–40. PMID 10477615.
- Donaldson EA, McKenna DJ, McMullen CB, Scott WN, Stitt AW, Nelson J (2000). "The expression of membrane-associated 67-kDa laminin receptor (67LR) is modulated in vitro by cell-contact inhibition". Mol. Cell Biol. Res. Commun. 3 (1): 53–59. doi:10.1006/mcbr.2000.0191. PMID 10683318.
- Pedraza C, Geberhiwot T, Ingerpuu S, Assefa D, Wondimu Z, Kortesmaa J, Tryggvason K, Virtanen I, Patarroyo M (2000). "Monocytic cells synthesize, adhere to, and migrate on laminin-8 (alpha 4 beta 1 gamma 1)". J. Immunol. 165 (10): 5831–8. doi:10.4049/jimmunol.165.10.5831. PMID 11067943.
- Vande Broek I, Vanderkerken K, De Greef C, Asosingh K, Straetmans N, Van Camp B, Van Riet I (2001). "Laminin-1-induced migration of multiple myeloma cells involves the high-affinity 67 kD laminin receptor". Br. J. Cancer. 85 (9): 1387–1395. doi:10.1054/bjoc.2001.2078. PMC 2375239. PMID 11720479.
- Waltregny D, de Leval L, Coppens L, Youssef E, de Leval J, Castronovo V (2002). "Detection of the 67-kD laminin receptor in prostate cancer biopsies as a predictor of recurrence after radical prostatectomy". Eur. Urol. 40 (5): 495–503. doi:10.1159/000049825. PMID 11752855.
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