Cytokines & Cells Online Pathfinder Encyclopaedia
|
Horst Ibelgaufts' COPE:
Cytokines & Cells Online Pathfinder Encyclopaedia |
 |
 |
 |
 |
 |
|
|
| COPE Homepage | Bottom of page | Previous entry: Juxtacrine |
Next entry: juxtaparenchymal cells |
Random entry: vCKBP-2 |
These cells are part of the vascular component of the juxtaglomerular apparatus, which is important in the maintenance of body salt-water homeostasis (Barajas, 1997). They are located in the media of the afferent arteriole at the entrance to the glomerulus in the kidney. These cells are specialized myoepithelioid cells. The individual renin secreting cell is a modified vascular smooth muscle cell. Juxtaglomerular cells are more highly differentiated than ordinary smooth muscle cells and contain numerous secretory granules (Biava and West, 1966; Hartroft and Newmark, 1961; Ishii and Fujimoto, 1968). Sequeira et al (2001) have reported that juxtaglomerular cells originate from the metanephric mesenchyme rather than from an extrarenal source.
The main function of juxtaglomerular cells is the synthesis, storage, and release of renin, the key hormone of the renin-angiotensin system that regulates arterial blood pressure (Hartroft et al, 1964; Schweda and Kurtz, 2004). The generation of transgenic mice expressing the human renin gene confirms that renin expression in the transgenic mouse kidney is confined to juxtaglomerular cells (Fukamizu et al, 1991). Juxtaglomerular cells also act as progenitor cells for another cell type and can transform into smooth muscle cells (which can convert also into juxtaglomerular cells) (Sequeira Lopez et al, 2001).
Clark et al (1997) have reported that knock-out mice lacking the Ren-1(d) gene, one of two mouse genes encoding renin, show an altered morphology of the macula densa of the kidney distal tubule and complete absence of juxtaglomerular cell granulation. These mice also exhibit sexually dimorphic hypotension. Cell ablation studies with transgenic mice lacking renin-expressing juxtaglomerular cells have shown that the absence of these cells affects morphology and functios. Homozygous mice survive normally, but have small kidneys. 25 % of the glomeruli are hyperplastic or atrophic, tubules are dilated and atrophic, and areas of undifferentiated cells exist near the atrophic glomeruli and tubules. Kidney vessels in homozygotes appear normal Homozygotes have severely reduced kidney and plasma renin concentrations. Females have reduced blood pressure. Homozygotes have elevated blood urea nitrogen and potassium levels. The authors have concluded that these cells are necessary for the morphological integrity of the kidney and may have a role in maintenance of normal kidney function (Pentz et al, 2004).
Juxtaglomerular cells have been shown to possess the capacity to express the proteins listed below. Please note the following general observation: expression may be influenced by tissue localization, may occur only in discrete subpopulations of cells, may vary between established cell lines, primary cells, embryonic cells, mature cells, fully differentiated cells, activated cells, non-activated cells or growth conditions (confluent vs. sparse cultures), may be influenced by various disease states (including cancer environment), and may differ between species.
Note also: expression profile information lists entities only for which there is an entry in COPE or one of its subdictionaries.
The meaning of • and •• is as follows: • factor/protein is expressed; •• receptor (or, in some instances, binding sites) for this factor/protein is expressed. For further explanations concerning format, "hidden" information, and/or ambiguities see my remarks in the entry cell types.
•• Adrenomedullin (ADM, AM) receptors (Jensen et al, 1997)
•• ANF (Atrial natriuretic factor, natriuretic peptide, atrionatriuretic factor, Alpha-ANP, Atrial natriuretic polypeptide, ANP, Atrial polypeptide, Atriopeptin, cardionatrin, cardionatrin I, NPPA) receptors (Kurtz et al, 1986; Naruse et al, 1988; Obana et al, 1985)
• angiotensin-1 (angiotensin) (Inagami et al, 1983, 1990; Rightsel et al, 1982)
• angiotensin-2 (Brooks et al, 1982; Inagami et al, 1990, 1991; Kurtz et al, 1986; Mercure et al, 1998; Rightsel et al, 1982)
•• angiotensin-2 receptors (Gasc et al, 1994; Ichihara et al, 2003; Kurtz and Penner, 1990)
•• Calcitonin gene-related peptide (CALC1, CALCA, Calcitonin gene-related polypeptide-alpha, alpha-CGRP, CGRP-alpha, beta-CGRP, CGRP-beta) receptors (Kurtz et al, 1988)
• cathepsin B (Neves et al, 1996)
• CD143 (ACE, angiotensin converting enzyme, angiotensin-1 converting enzyme, dipeptidyl carboxypeptidase, dipeptidyl carboxypeptidase 1, EC3.4.15.1, kininase 2, peptidase P, peptidyl dipeptidase A) (Rightsel et al, 1982)
•• EGF (epidermal growth factor, EGF-URO, HMGF, human milk growth factor, PGF, prostatic growth factor, beta-Urogastrone, URO, URG, Urogastrone, tooth-lid factor) receptors (erb, erbB1, HER1) (Toubeau et al, 1994)
• endothelin-1 (ET-1(1-21), ET-1) (Chen et al, 1993; Yanagisawa et al, 1998)
•• endothelin-1 (ET-1(1-21), ET-1) receptors (Chao et al, 1993; Kramer et al, 1996; Ritthaler et al, 1996)
•• endothelin-2 (ET-2) receptors (Chao et al, 1993; Kramer et al, 1996; Chao et al, 1993)
•• endothelin-3 (ET-3) receptors (Kramer et al, 1996)
•• IL1-beta (IL1B, interleukin-1-beta, Catabolin, H1, Hematopoietin-1, IFN-beta inducing factor, Interleukin-beta, OAF, osteoclast activating factor) receptors (IL1R, IL1RA, IL1R1, IL1 receptor type 1, IL1RB, IL1R2, IL1 receptor type 2, CD121a, CD121b) (Galle et al, 1995; Jensen et al, 1998)
•• Oncostatin M (OSM, OM, Onco M, OnM) receptors (Baumann et al, 2000)
• PAMP-20 (Baumann et al, 2000)
• parathyroid hormone receptors (Saussine et al, 1993)
• PDGF (platelet-derived growth factor, PDGF-1, PDGF-2, PDGF-A, PDGF-AA, PDGF-B, PDGF-BB, FDGF, fibroblast-derived growth factor, GDGF, glioma-derived growth factor-1, GDGF-2, glioma-derived growth factor-2, GSM, Glucocorticoid-suppressible mitogenic activity, MDF, mesangial cell proliferating factor, MDGF, monocyte-derived growth factor, OBIF, osteoblastogenesis inhibitory factor, ODGF, osteosarcoma-derived growth factor, T47D factor) (Shehata et al, 1995)
• TGF-beta-1 (transforming growth factor-beta-1, CIF-A, cartilage inducing factor A, ISF, immunosuppressive factor, MGF-b, milk growth factor, PDGI, platelet-derived endothelial cell growth inhibitor) (Shehata et al, 1995)
•• TGF-beta-1 (transforming growth factor-beta-1, CIF-A, cartilage inducing factor A, ISF, immunosuppressive factor, MGF-b, milk growth factor, PDGI, platelet-derived endothelial cell growth inhibitor) receptors (Antonipillai et al, 1993)
•• TGF-beta-2 (transforming growth factor-beta-2, TGFB2, G-TsF, Glioblastoma-derived T-cell suppressor factor, CIF-B, cartilage inducing factor B, Corneal epithelial inhibitor of stromal cell collagenase synthesis, DSF, decidual suppressor factor, MGF-a, milk growth factor) receptors (Antonipillai et al, 1993)
•• TGF-beta (transforming growth factor-beta, TGFB, B-TGF, Aqueous humor lymphocyte inhibitory activity, DIF, differentiation-inhibiting factor, EGI, epithelial cell-specific growth inhibitor; epithelial growth inhibitor, EIF, Epstein-Barr virus inducing factor, Epithelial cell growth inhibiting factor, G-TsF, glioma-derived T-cell suppressor factor, MDGF, milk-derived growth factor, MGF, milk growth factor, Polyergin, Simian BSC-1 cell growth inhibitor, SP factor, TCGF, transformed cell growth factor, TGI, tissue-derived growth inhibitor, TIF-1, tumor inducing factor-1) receptors (Liu and Ballermann, 1998)
•• TNF-alpha (tumor necrosis factor-alpha, TNFSF2, TNF ligand superfamily member 2, Cachectin, CF, cytotoxic factor, CTX, cytotoxin, DIF, differentiation inducing factor, EP, endogenous pyrogens, Hemorrhagic factor, Macrophage-derived cytotoxic factor, J774-derived cytotoxic factor, MCF, macrophage cytotoxic factor, MCT, macrophage cytotoxin, MD-FGF, monocyte-derived fibroblast growth factor, PCF, peritoneal cytotoxic factor, RCF, Released cytotoxic factor) receptors (Todorov et al, 2004)
•• Vasopressin (Arginine vasopressin, Arg-Vasopressin, AVP, ARVP, VP, Antidiuretic hormone, ADH, Adiuretin, Vasotocin, Pituitrin P, Pitressin, arginine-vasopressin-neurophysin II, vasopressin-neurophysin 2-copeptin, AVP-NpII) receptors (Kurtz et al, 1986)
•• VIP (vasoactive intestinal peptide) receptors (Porter and Ganong, 1988; Porter et al, 1983)
For related information see also: Cell types.
LAST MODIFIED: September 2006
See REFERENCES for entry juxtaglomerular cells
| COPE Homepage | Top of Page |
| SUPPORT COPE | Intro | Subdictionaries | New Entries | Contribute data | COPE Credentials |
| # | A | B | C | D | E | F | G | H | I | J | K | L | M | N | O | P | Q | R | S | T | U | V | W | X | Y | Z |
|
Space for your TEXTLINK ADVERTISEMENTS. Please Inquire
|
 |
 |
 |
 |
 |
 |
 |
supports the COPE bioinformatics project with an unrestricted educational grant |
Created, developed, and maintained by Prof Dr H Ibelgaufts
|
| Access to COPE is free only for academic institutions and non-profit organizations. OTHER USERS: must contact COPE and pay a site licence fee. Non-payment of the site licence fee is a serious breach of COPE's binding Usage Agreement. If you do not wish to be bound by this agreement, do not use COPE |
| COPE is not in the public domain! The commercial use of COPE contents is not allowed. Download of complete offline-readable copies and the use of automatic extraction methods are prohibited! Usage Agreement, Disclaimer, Copyright Notice | All rights reserved by H Ibelgaufts | Privacy Statement U L T R A P O S S E N E M O O B L I G A T U R |