Podocalyxin-like protein 1 is a
protein that in humans is encoded by the PODXLgene.[3]
Function
This gene encodes a member of the CD34 sialomucin protein family.[4] The encoded protein was originally identified as an important component of glomerular podocytes. Inactivation of the encoding gene in mice leads to anuria, omphalocele and perinatal death.[5] Podocytes are highly differentiated epithelial cells with interdigitating foot processes covering the outer aspect of the glomerular basement membrane. Other biological activities of the encoded protein include: binding in a membrane protein complex with Na+/H+ exchanger regulatory factor to intracellular cytoskeletal elements, playing a role in hematopoietic cell differentiation, and being expressed in vascular endothelium cells and binding to L-selectin.[3]
Podocalyxin is upregulated in a number of cancers and is frequently associated with poor prognosis.[13] Based on patient survival data,[14] high level of PODXL transcripts in tumor cells is associated with poor prognosis in
renal cancer.
^Li Y, Li J, Straight SW, Kershaw DB (Jun 2002). "PDZ domain-mediated interaction of rabbit podocalyxin and Na(+)/H(+) exchange regulatory factor-2". American Journal of Physiology. Renal Physiology. 282 (6): F1129–39.
doi:
10.1152/ajprenal.00131.2001.
PMID11997330.
Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4.
doi:
10.1016/0378-1119(94)90802-8.
PMID8125298.
Kershaw DB, Wiggins JE, Wharram BL, Wiggins RC (Oct 1997). "Assignment of the human podocalyxin-like protein (PODXL) gene to 7q32-q33". Genomics. 45 (1): 239–40.
doi:
10.1006/geno.1997.4934.
PMID9339384.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56.
doi:
10.1016/S0378-1119(97)00411-3.
PMID9373149.
Li Y, Li J, Straight SW, Kershaw DB (Jun 2002). "PDZ domain-mediated interaction of rabbit podocalyxin and Na(+)/H(+) exchange regulatory factor-2". American Journal of Physiology. Renal Physiology. 282 (6): F1129–39.
doi:
10.1152/ajprenal.00131.2001.
PMID11997330.
Schopperle WM, Kershaw DB, DeWolf WC (Jan 2003). "Human embryonal carcinoma tumor antigen, Gp200/GCTM-2, is podocalyxin". Biochemical and Biophysical Research Communications. 300 (2): 285–90.
doi:
10.1016/S0006-291X(02)02844-9.
PMID12504081.
Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (Jun 2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nature Biotechnology. 22 (6): 707–16.
doi:
10.1038/nbt971.
PMID15146197.
S2CID27764390.
Economou CG, Kitsiou PV, Tzinia AK, Panagopoulou E, Marinos E, Kershaw DB, Kerjaschki D, Tsilibary EC (Jul 2004). "Enhanced podocalyxin expression alters the structure of podocyte basal surface". Journal of Cell Science. 117 (Pt 15): 3281–94.
doi:
10.1242/jcs.01163.
PMID15226400.
S2CID13492264.
Somasiri A, Nielsen JS, Makretsov N, McCoy ML, Prentice L, Gilks CB, Chia SK, Gelmon KA, Kershaw DB, Huntsman DG, McNagny KM, Roskelley CD (Aug 2004). "Overexpression of the anti-adhesin podocalyxin is an independent predictor of breast cancer progression". Cancer Research. 64 (15): 5068–73.
doi:
10.1158/0008-5472.CAN-04-0240.
hdl:1807.1/116.
PMID15289306.
S2CID15399303.
Podocalyxin-like protein 1 is a
protein that in humans is encoded by the PODXLgene.[3]
Function
This gene encodes a member of the CD34 sialomucin protein family.[4] The encoded protein was originally identified as an important component of glomerular podocytes. Inactivation of the encoding gene in mice leads to anuria, omphalocele and perinatal death.[5] Podocytes are highly differentiated epithelial cells with interdigitating foot processes covering the outer aspect of the glomerular basement membrane. Other biological activities of the encoded protein include: binding in a membrane protein complex with Na+/H+ exchanger regulatory factor to intracellular cytoskeletal elements, playing a role in hematopoietic cell differentiation, and being expressed in vascular endothelium cells and binding to L-selectin.[3]
Podocalyxin is upregulated in a number of cancers and is frequently associated with poor prognosis.[13] Based on patient survival data,[14] high level of PODXL transcripts in tumor cells is associated with poor prognosis in
renal cancer.
^Li Y, Li J, Straight SW, Kershaw DB (Jun 2002). "PDZ domain-mediated interaction of rabbit podocalyxin and Na(+)/H(+) exchange regulatory factor-2". American Journal of Physiology. Renal Physiology. 282 (6): F1129–39.
doi:
10.1152/ajprenal.00131.2001.
PMID11997330.
Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4.
doi:
10.1016/0378-1119(94)90802-8.
PMID8125298.
Kershaw DB, Wiggins JE, Wharram BL, Wiggins RC (Oct 1997). "Assignment of the human podocalyxin-like protein (PODXL) gene to 7q32-q33". Genomics. 45 (1): 239–40.
doi:
10.1006/geno.1997.4934.
PMID9339384.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56.
doi:
10.1016/S0378-1119(97)00411-3.
PMID9373149.
Li Y, Li J, Straight SW, Kershaw DB (Jun 2002). "PDZ domain-mediated interaction of rabbit podocalyxin and Na(+)/H(+) exchange regulatory factor-2". American Journal of Physiology. Renal Physiology. 282 (6): F1129–39.
doi:
10.1152/ajprenal.00131.2001.
PMID11997330.
Schopperle WM, Kershaw DB, DeWolf WC (Jan 2003). "Human embryonal carcinoma tumor antigen, Gp200/GCTM-2, is podocalyxin". Biochemical and Biophysical Research Communications. 300 (2): 285–90.
doi:
10.1016/S0006-291X(02)02844-9.
PMID12504081.
Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (Jun 2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nature Biotechnology. 22 (6): 707–16.
doi:
10.1038/nbt971.
PMID15146197.
S2CID27764390.
Economou CG, Kitsiou PV, Tzinia AK, Panagopoulou E, Marinos E, Kershaw DB, Kerjaschki D, Tsilibary EC (Jul 2004). "Enhanced podocalyxin expression alters the structure of podocyte basal surface". Journal of Cell Science. 117 (Pt 15): 3281–94.
doi:
10.1242/jcs.01163.
PMID15226400.
S2CID13492264.
Somasiri A, Nielsen JS, Makretsov N, McCoy ML, Prentice L, Gilks CB, Chia SK, Gelmon KA, Kershaw DB, Huntsman DG, McNagny KM, Roskelley CD (Aug 2004). "Overexpression of the anti-adhesin podocalyxin is an independent predictor of breast cancer progression". Cancer Research. 64 (15): 5068–73.
doi:
10.1158/0008-5472.CAN-04-0240.
hdl:1807.1/116.
PMID15289306.
S2CID15399303.