PMID- 10504499
OWN - NLM
STAT- MEDLINE
DCOM- 19991202
LR  - 20071114
IS  - 0085-2538 (Print)
IS  - 0085-2538 (Linking)
VI  - 56
IP  - 4
DP  - 1999 Oct
TI  - Nephrin localizes to the slit pore of the glomerular epithelial cell.
PG  - 1481-91
AB  - BACKGROUND: Recognition that mutation of the protein nephrin, encoded by the
      NPHS1 gene, singly results in the cellular alterations that result in foot
      process effacement, and nephrotic range proteinuria emphasizes the pivotal role
      that this protein plays in regulating glomerular filter integrity. This article
      reports the development of reagents necessary to study the biology of nephrin in 
      mouse, and describes the initial characterization of the nephrin protein.
      METHODS: A cDNA including the full-length mouse nephrin open reading frame was
      cloned and sequenced. Immuno-affinity purified polyclonal antiserum directed
      against the cytoplasmic domain of mouse nephrin was developed. RESULTS: Nephrin
      identified in mouse glomerular extract was found to be a glycoprotein with an
      apparent molecular mass of 185 kDa. As detected by indirect immunofluorescence
      microscopy and immunogold electron microscopy, nephrin was located only in
      visceral glomerular epithelial cells, where it was targeted to intercellular
      junctions of mature podocyte foot processes. In developing glomeruli of newborn
      mouse, antinephrin immunolocalized to the earliest slit pore regions between
      differentiating podocytes, sites where slit diaphragms first become visible.
      CONCLUSION: As a putative cell adhesion molecule of the immunoglobulin
      superfamily, nephrin likely participates in cell-cell interactions between
      podocyte foot processes and may represent a component of the slit diaphragm.
FAU - Holzman, L B
AU  - Holzman LB
AD  - University of Michigan Medical School, 1560 Medical Science Research Building II,
      Ann Arbor 48109-0676, USA. lholzman@umich.edu
FAU - St John, P L
AU  - St John PL
FAU - Kovari, I A
AU  - Kovari IA
FAU - Verma, R
AU  - Verma R
FAU - Holthofer, H
AU  - Holthofer H
FAU - Abrahamson, D R
AU  - Abrahamson DR
LA  - eng
SI  - GENBANK/AF168466
GR  - DK-34972/DK/NIDDK NIH HHS/United States
GR  - DK-47566/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Kidney Int
JT  - Kidney international
JID - 0323470
RN  - 0 (DNA, Complementary)
RN  - 0 (Membrane Proteins)
RN  - 0 (Proteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (nephrin)
SB  - IM
MH  - Age Factors
MH  - Animals
MH  - Animals, Newborn
MH  - Blotting, Northern
MH  - Cell Communication/physiology
MH  - Cloning, Molecular
MH  - DNA, Complementary
MH  - Epithelial Cells/*chemistry/physiology/ultrastructure
MH  - Fluorescent Antibody Technique
MH  - Gene Expression/physiology
MH  - Intercellular Junctions/*chemistry
MH  - Kidney Glomerulus/*cytology/growth & development
MH  - Membrane Proteins
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Microscopy, Electron
MH  - Molecular Sequence Data
MH  - Proteins/*analysis/*genetics
MH  - RNA, Messenger/analysis
MH  - Sequence Homology, Amino Acid
MH  - Transcription, Genetic/physiology
EDAT- 1999/10/03 00:00
MHDA- 1999/10/03 00:01
CRDT- 1999/10/03 00:00
PHST- 1999/10/03 00:00 [pubmed]
PHST- 1999/10/03 00:01 [medline]
PHST- 1999/10/03 00:00 [entrez]
AID - S0085-2538(15)46456-7 [pii]
AID - 10.1046/j.1523-1755.1999.00719.x [doi]
PST - ppublish
SO  - Kidney Int. 1999 Oct;56(4):1481-91. doi: 10.1046/j.1523-1755.1999.00719.x.