AAMP (gene)

Last updated
AAMP
Identifiers
Aliases AAMP , angio associated migratory cell protein
External IDs OMIM: 603488 MGI: 107809 HomoloGene: 846 GeneCards: AAMP
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001302545
NM_001087

NM_001190444
NM_146110

RefSeq (protein)

NP_001078
NP_001289474

n/a

Location (UCSC) Chr 2: 218.26 – 218.27 Mb Chr 1: 74.32 – 74.32 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Angio-associated, migratory cell protein, also known as AAMP, is a protein which in humans is encoded by the AAMP gene. [5] This protein has been conserved in evolution and is so common to many mammals. [6] and it also has a yeast homolog which is the protein YCR072c. [7] [8]

Contents

Localisation

The gene is located on the second human chromosome, near the end of the chromosome's arm (2q35), between the codons 85-87 and 1387–1389. It contains 6042 bp and 11 exons [6] When transcribed, it gives a 1859 bp mRNA. . [6] The vascular endothelial growth factor is a promoting factor of the protein synthesis and localisation in the different parts of the cells. [9] The protein's expression is higher in the intracellular than in the extracellular space. [7]

Function

The gene product is an immunoglobulin-type protein of 434 amino acids and 49 kDa. [6] It is found to be expressed strongly in the cytosol of endothelial cells, cytotrophoblasts, and poorly differentiated colon adenocarcinoma cells found in lymphatics and has been observed at the luminal edges of endometrial cells and in the extracellular environment of vascular-associated mesenchymal cells. [6]

The protein contains a WD40 domain which permits multi-proteins complexes formation [6] and a heparin-binding domain which mediates heparin-sensitive cell adhesion. [5] AAMP helps to regulate vascular endothelial cell migration regulation and angiogenesis, with other signaling pathway like RhoA/Rho-kinase signaling. [9] A malfunction can therefore lead to different diseases (see Associated diseases). For example, in the smooth muscle cells, if AAMP is overexpressed, it activates RhoA, which activates Rho-kinase (this one generates GTP) and it finally leads to increased smooth muscle cell migration and division, causing atherosclerosis and restenosis. [10]

Associated diseases

Note : In all these diseases [6] we can observe the expression of the AAMP gene. This one can either remain stable, increase or decrease depending on the disease.

List of the diseases : gastrointestinal stromal tumor (GIST) (for this disease and the ductal carcinomas, the expression levels are to correlate with necrosis in situ [11] ), myeloid leukemia (chronic (CML) and acute (AML) forms), lymphoma, breast cancer, glial brain tumors, colon neoplasia, epidermoid carcinoma, cervical cancer, ovarian cancer, papillary thyroid cancer, pulmonary cancer, atherosclerosis, restenosis.

Related Research Articles

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<span class="mw-page-title-main">Angiogenin</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">CTGF</span>

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<span class="mw-page-title-main">Heparin-binding EGF-like growth factor</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">ROCK1</span> Protein

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<span class="mw-page-title-main">Peptidylprolyl isomerase A</span>

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<span class="mw-page-title-main">GPR56</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">Placental growth factor</span>

Placental growth factor(PlGF) is a protein that in humans is encoded by the PGF gene.

<span class="mw-page-title-main">C-fos-induced growth factor</span> Mammalian protein found in Homo sapiens

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<span class="mw-page-title-main">NRCAM</span>

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<span class="mw-page-title-main">Discoidin domain-containing receptor 2</span>

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<span class="mw-page-title-main">MAP4K4</span>

Mitogen-activated protein kinase kinase kinase kinase 4 (MAP4K4) – also known as hepatocyte progenitor kinase-like/germinal center kinase-like kinase (HGK) and Nck-interacting kinase (NIK) – is an enzyme, specifically a serine/threonine (S/T) kinase encoded by the MAP4K4 gene in humans.

<span class="mw-page-title-main">Vascular endothelial growth factor A</span> Protein involved in blood vessel growth

Vascular endothelial growth factor A (VEGF-A) is a protein that in humans is encoded by the VEGFA gene.

<span class="mw-page-title-main">TIE1</span>

Tyrosine kinase with immunoglobulin-like and EGF-like domains 1 also known as TIE1 is an angiopoietin receptor which in humans is encoded by the TIE1 gene.

Angiogenesis is the process of forming new blood vessels from existing blood vessels. It is a highly complex process involving extensive interplay between cells, soluble factors, and the extracellular matrix (ECM). Angiogenesis is critical during normal physiological development, but it also occurs in adults during inflammation, wound healing, ischemia, and in pathological conditions such as rheumatoid arthritis, hemangioma, and tumor growth. Proteolysis has been indicated as one of the first and most sustained activities involved in the formation of new blood vessels. Numerous proteases including matrix metalloproteases (MMPs), a disintegrin and metalloprotease domain (ADAM), a disintegrin and metalloprotease domain with throbospondin motifs (ADAMTS), and cysteine and serine proteases are involved in angiogenesis. This article focuses on the important and diverse roles that these proteases play in the regulation of angiogenesis.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000127837 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000006299 - 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. 1 2 "Entrez Gene: AAMP angio-associated, migratory cell protein".
  6. 1 2 3 4 5 6 7 Beckner ME (March 2012). "AAMP (angio-associated, migratory cell protein)". Atlas of Genetics and Cytogenetics in Oncology and Haematology. 16 (2): 111–114. doi: 10.4267/2042/46939 .
  7. 1 2 Beckner ME, Peterson VA, Moul DE (1999). "Angio-associated migratory cell protein is expressed as an extracellular protein by blood-vessel-associated mesenchymal cells". Microvascular Research. 57 (3): 347–52. doi:10.1006/mvre.1999.2144. PMID   10329261.
  8. Beckner ME, Liotta LA (July 1996). "AAMP, a conserved protein with immunoglobulin and WD40 domains, regulates endothelial tube formation in vitro". Laboratory Investigation; A Journal of Technical Methods and Pathology. 75 (1): 97–107. PMID   8683944.
  9. 1 2 Hu J, Qiu J, Zheng Y, Zhang T, Yin T, Xie X, Wang G (May 2016). "AAMP Regulates Endothelial Cell Migration and Angiogenesis Through RhoA/Rho Kinase Signaling". Annals of Biomedical Engineering. 44 (5): 1462–74. doi:10.1007/s10439-015-1442-0. PMID   26350504. S2CID   52810718.
  10. Holvoet P, Sinnaeve P (July 2008). "Angio-associated migratory cell protein and smooth muscle cell migration in development of restenosis and atherosclerosis". Journal of the American College of Cardiology. 52 (4): 312–4. doi: 10.1016/j.jacc.2008.04.024 . PMID   18634988.
  11. Bielig H, Zurek B, Kutsch A, Menning M, Philpott DJ, Sansonetti PJ, Kufer TA (August 2009). "A function for AAMP in Nod2-mediated NF-kappaB activation". Molecular Immunology. 46 (13): 2647–54. doi:10.1016/j.molimm.2009.04.022. PMID   19535145.

Further reading