Podoplanin

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Podoplanin
Properties of human protein
Mass / length primary structure 140 amino acids
Secondary to quaternary structure Membrane protein
Isoforms hT1α-1; hT1α-2
Identifier
Gene names PDPN  ; T1A; Gp36
External IDs
Occurrence
Homology family Podoplanin
Parent taxon Higher mammals
Orthologue
human House mouse
Entrez 10630 14726
Ensemble ENSG00000162493 ENSMUSG00000028583
UniProt Q86YL7 Q62011
Refseq (mRNA) NM_001006624 NM_001290822
Refseq (protein) NP_001006625 NP_001277751
Gene locus Chr 1: 13.58 - 13.62 Mb Chr 4: 143.27 - 143.3 Mb
PubMed search 10630 14726

Podoplanin is a membrane glycoprotein that in various tissues in the human body expressed , for example, is kidney - podocytes was named, according to which it.

Since podoplanin is strongly expressed on lymphatic endothelial cells but not on blood endothelial cells, it serves as a marker for lymphatic vessels. The exact physiological function of podoplanin is unknown. However, experiments with podoplanin knockout mice have shown that the protein is involved in the development of the lungs and the lymphatic vasculature.

There are several alternatively spliced ​​transcript variants which encode isoforms of different lengths.

Podoplanin binds to the platelet receptor CLEC-2 in mice and humans. Podoplanin knockout mice show developmental damage to the heart. In patients with primary brain tumors, increased podoplanin expression is associated with an increased risk of venous thromboembolism . Podoplanin is a marker for oral cancer risk.

In addition, podoplanin activates the intracellular GTPase RhoA via binding to ERM proteins colocalized with podoplanin, such as ezrin.

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  1. ↑ Breiteneder-Geleff, S., et al., Podoplanin, novel 43-kd membrane protein of glomerular epithelial cells, is down-regulated in puromycin nephrosis. In: Am J Pathol , 1997. 151 (4): p. 1141-52
  2. ↑ Baluk P, McDonald DM: Markers for microscopic imaging of lymphangiogenesis and angiogenesis . In: Ann. NY Acad. Sci. . 1131, 2008, pp. 1-12. doi : 10.1196 / annals.1413.001 . PMID 18519955 .
  3. ↑ Ramirez MI, et al., T1alpha, a lung type I cell differentiation gene, is required for normal lung cell proliferation and alveolus formation at birth. In: Dev Biol , 2003 Apr 1; ​​256 (1): 61-72
  4. ↑ Schacht, V., et al., T1alpha / podoplanin deficiency disrupts normal lymphatic vasculature formation and causes lymph-edema. In: Embo J , 2003. 22 (14): p. 3546-56
  5. ↑ Julia Riedl, Matthias Preusser, Pegah Mir Seyed Nazari, Florian Posch, Simon Panzer: Podoplanin expression in primary brain tumors induces platelet aggregation and increases risk of venous thromboembolism . In: Blood . tape 129 , no. 13 , March 30, 2017, ISSN  0006-4971 , p. 1831-1839 , doi : 10.1182 / blood-2016-06-720714 , PMID 28073783 ( bloodjournal.org [accessed May 3, 2017]).
  6. ↑ Xie J, Wu T, Guo L, et al : Molecular characterization of two novel isoforms and a soluble form of mouse CLEC-2 . In: Biochem. Biophys. Res. Commun. . 371, No. 2, June 2008, pp. 180-4. doi : 10.1016 / j.bbrc.2008.03.070 . PMID 18361921 .
  7. ↑ Christou CM, Pearce AC, Watson AA, et al : Renal cells activate the platelet receptor CLEC-2 through podoplanin . In: Biochem. J. . 411, No. 1, April 2008, pp. 133-40. doi : 10.1042 / BJ20071216 . PMID 18215137 .
  8. ↑ Mahtab EA, Wijffels MC, Van Den Akker NM, et al : Cardiac malformations and myocardial abnormalities in podoplanin knockout mouse embryos: Correlation with abnormal epicardial development . In: Dev. Dyn. . 237, No. 3, March 2008, pp. 847-57. doi : 10.1002 / dvdy.21463 . PMID 18265012 .
  9. ↑ Kawaguchi H, El-Naggar AK, Papadimitrakopoulou V, et al : Podoplanin: a novel marker for oral cancer risk in patients with oral premalignancy . In: J. Clin. Oncol. . 26, No. 3, January 2008, pp. 354-60. doi : 10.1200 / JCO.2007.13.4072 . PMID 18202409 .
  10. ↑ Martin-Villar E, et al., Podoplanin binds ERM proteins to activate RhoA and promote epithelial-mesenchymal transition , In: J Cell Sci , 2006 Nov 1; 119 (Pt 21): 4541-53. Epub 2006 Oct 17, PMID 17046996