MMP10

MMP10

Matrix metallopeptidase 10 (stromelysin 2), also known as MMP10, is a human gene.

PBB_Summary
section_title =
summary_text = Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades proteoglycans and fibronectin. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.cite web | title = Entrez Gene: MMP10 matrix metallopeptidase 10 (stromelysin 2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4319| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Chandler S, Miller KM, Clements JM, "et al." |title=Matrix metalloproteinases, tumor necrosis factor and multiple sclerosis: an overview. |journal=J. Neuroimmunol. |volume=72 |issue= 2 |pages= 155–61 |year= 1997 |pmid= 9042108 |doi=
*cite journal | author=Nagase H, Woessner JF |title=Matrix metalloproteinases. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21491–4 |year= 1999 |pmid= 10419448 |doi=
*cite journal | author=Fosang AJ, Neame PJ, Hardingham TE, "et al." |title=Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins. |journal=J. Biol. Chem. |volume=266 |issue= 24 |pages= 15579–82 |year= 1991 |pmid= 1874716 |doi=
*cite journal | author=Jung JY, Warter S, Rumpler Y |title=Localization of stromelysin 2 gene to the q22.3-23 region of chromosome 11 by in situ hybridization. |journal=Ann. Genet. |volume=33 |issue= 1 |pages= 21–3 |year= 1990 |pmid= 2369069 |doi=
*cite journal | author=Sirum KL, Brinckerhoff CE |title=Cloning of the genes for human stromelysin and stromelysin 2: differential expression in rheumatoid synovial fibroblasts. |journal=Biochemistry |volume=28 |issue= 22 |pages= 8691–8 |year= 1990 |pmid= 2605216 |doi=
*cite journal | author=Muller D, Quantin B, Gesnel MC, "et al." |title=The collagenase gene family in humans consists of at least four members. |journal=Biochem. J. |volume=253 |issue= 1 |pages= 187–92 |year= 1988 |pmid= 2844164 |doi=
*cite journal | author=Lichtinghagen R, Helmbrecht T, Arndt B, Böker KH |title=Expression pattern of matrix metalloproteinases in human liver. |journal=European journal of clinical chemistry and clinical biochemistry : journal of the Forum of European Clinical Chemistry Societies |volume=33 |issue= 2 |pages= 65–71 |year= 1995 |pmid= 7632822 |doi=
*cite journal | author=Nguyen Q, Murphy G, Hughes CE, "et al." |title=Matrix metalloproteinases cleave at two distinct sites on human cartilage link protein. |journal=Biochem. J. |volume=295 ( Pt 2) |issue= |pages= 595–8 |year= 1993 |pmid= 7694569 |doi=
*cite journal | author=Conca W, Willmroth F |title=Human T lymphocytes express a member of the Matrix Metalloproteinase gene family. |journal=Arthritis Rheum. |volume=37 |issue= 6 |pages= 951–6 |year= 1994 |pmid= 8003069 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Gack S, Vallon R, Schaper J, "et al." |title=Phenotypic alterations in fos-transgenic mice correlate with changes in Fos/Jun-dependent collagenase type I expression. Regulation of mouse metalloproteinases by carcinogens, tumor promoters, cAMP, and Fos oncoprotein. |journal=J. Biol. Chem. |volume=269 |issue= 14 |pages= 10363–9 |year= 1994 |pmid= 8144618 |doi=
*cite journal | author=Windsor LJ, Grenett H, Birkedal-Hansen B, "et al." |title=Cell type-specific regulation of SL-1 and SL-2 genes. Induction of the SL-2 gene but not the SL-1 gene by human keratinocytes in response to cytokines and phorbolesters. |journal=J. Biol. Chem. |volume=268 |issue= 23 |pages= 17341–7 |year= 1993 |pmid= 8349617 |doi=
*cite journal | author=Knäuper V, Murphy G, Tschesche H |title=Activation of human neutrophil procollagenase by stromelysin 2. |journal=Eur. J. Biochem. |volume=235 |issue= 1-2 |pages= 187–91 |year= 1996 |pmid= 8631328 |doi=
*cite journal | author=Pendás AM, Santamaría I, Alvarez MV, "et al." |title=Fine physical mapping of the human matrix metalloproteinase genes clustered on chromosome 11q22.3. |journal=Genomics |volume=37 |issue= 2 |pages= 266–8 |year= 1997 |pmid= 8921407 |doi=
*cite journal | author=Sorsa T, Salo T, Koivunen E, "et al." |title=Activation of type IV procollagenases by human tumor-associated trypsin-2. |journal=J. Biol. Chem. |volume=272 |issue= 34 |pages= 21067–74 |year= 1997 |pmid= 9261109 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Madlener M, Werner S |title=cDNA cloning and expression of the gene encoding murine stromelysin-2 (MMP-10). |journal=Gene |volume=202 |issue= 1-2 |pages= 75–81 |year= 1998 |pmid= 9427548 |doi=
*cite journal | author=Nakamura H, Fujii Y, Ohuchi E, "et al." |title=Activation of the precursor of human stromelysin 2 and its interactions with other matrix metalloproteinases. |journal=Eur. J. Biochem. |volume=253 |issue= 1 |pages= 67–75 |year= 1998 |pmid= 9578462 |doi=
*cite journal | author=Bord S, Horner A, Hembry RM, Compston JE |title=Stromelysin-1 (MMP-3) and stromelysin-2 (MMP-10) expression in developing human bone: potential roles in skeletal development. |journal=Bone |volume=23 |issue= 1 |pages= 7–12 |year= 1998 |pmid= 9662124 |doi=

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Нужен реферат?

Look at other dictionaries:

  • Matrix metalloproteinase — Cell surface associated MT1 MMP (MMP14), Green fluorescent protein (GFP) fused to the C term produces a signal on the surface of the cell[1] Matrix metalloproteinases (MMPs) are zinc dependent endopeptidases; other family members are adamalysins …   Wikipedia

  • Metalloendopeptidase — A metalloendopeptidase is an enzyme that functions as a metalloproteinase endopeptidase. External links MeSH Metalloendopeptidase 3.4.21 24: Endopeptidase …   Wikipedia

  • Collagenase — matrix metallopeptidase 1 (interstitial collagenase) Identifiers Symbol MMP1 Entrez 4312 HUGO …   Wikipedia

  • ADAM17 — ADAM metallopeptidase domain 17 PDB rendering based on 1bkc …   Wikipedia

  • Neprilysin — Membrane metallo endopeptidase The structure of the neprilysin ectodomain in complex with a zinc chelating inhibitor. The zinc atom is shown as a gray sphere and the inhibitor is shown in green. Rendering based on 1r1h …   Wikipedia

  • Pregnancy-associated plasma protein A — Pregnancy associated plasma protein A, pappalysin 1 Identifiers Symbols PAPPA; ASBABP2; DIPLA1; IGFBP 4ase; PAPA; PAPP A; PAPPA1 External IDs …   Wikipedia

  • MMP14 — Matrix metallopeptidase 14 (membrane inserted) PDB rendering based on 1bqq …   Wikipedia

  • MMP1 — Matrix metallopeptidase 1 (interstitial collagenase) PDB rendering based on 1ayk …   Wikipedia

  • MMP3 — Matrix metallopeptidase 3 (stromelysin 1, progelatinase) PDB rendering based on 1b3d …   Wikipedia

  • MMP7 — Matrix metallopeptidase 7 (matrilysin, uterine) PDB rendering based on 1mmp …   Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”