PMID- 10548494
OWN - NLM
STAT- MEDLINE
DCOM- 19991217
LR  - 20061115
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 265
IP  - 1
DP  - 1999 Nov
TI  - Biochemical characterization and expression analysis of neural
      thrombospondin-1-like proteins NELL1 and NELL2.
PG  - 79-86
AB  - Two closely related genes coding for NELL proteins (NELL1 and NELL2) have been
      cloned by the yeast two-hybrid screening of a rat brain cDNA library with the
      regulatory domain of protein kinase C betaI (PKCbetaI) as bait. The rat NELL
      proteins show about 55% identity with each other and contain several protein
      motifs assigned to a secretion signal peptide, an NH(2)-terminal thrombospondin-1
      (TSP-1)-like module, five von Willebrand factor C domains, and six epidermal
      growth factor-like domains; the NELL proteins share many protein motifs with
      TSP-1. The NELL proteins expressed in COS-7 cells are homotrimeric glycoproteins 
      and possess heparin-binding activity. Furthermore, while NELL1 and NELL2 show
      distinct subcellular localization in cytoplasm, they both are partially secreted 
      into the culture medium of COS-7 cells. Although the NELL1 mRNA is faintly
      expressed in adult neural cells, the NELL2 mRNA is expressed abundantly,
      particularly in the pyramidal cells of rat hippocampus, showing neuronal high
      plasticity. During mouse embryogenesis, expression of the NELL2 mRNA is initiated
      7-11 days postcoitum, simultaneously with neural plate formation. These results
      strongly suggest that the NELL2 protein, similar to but not identical with TSP-1,
      is involved in the growth and differentiation of neural cells. Additionally, the 
      NELL1 and NELL2 mRNAs were found to be expressed abundantly in Burkitt's lymphoma
      Raji cells and colorectal adenocarcinoma SW480 cells, respectively. Thus, it is
      likely that the NELL proteins also participate in the growth, differentiation,
      and oncogenesis of cancer cell lines.
CI  - Copyright 1999 Academic Press.
FAU - Kuroda, S
AU  - Kuroda S
AD  - Institute of Scientific and Industrial Research, Osaka University, Osaka,
      567-0047, Japan. skuroda@sanken.osakau.ac.jp
FAU - Oyasu, M
AU  - Oyasu M
FAU - Kawakami, M
AU  - Kawakami M
FAU - Kanayama, N
AU  - Kanayama N
FAU - Tanizawa, K
AU  - Tanizawa K
FAU - Saito, N
AU  - Saito N
FAU - Abe, T
AU  - Abe T
FAU - Matsuhashi, S
AU  - Matsuhashi S
FAU - Ting, K
AU  - Ting K
LA  - eng
SI  - GENBANK/U48245
SI  - GENBANK/U48246
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Nell1 protein, rat)
RN  - 0 (Nell2 protein, mouse)
RN  - 0 (Nell2 protein, rat)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Protein Sorting Signals)
RN  - 0 (RNA, Messenger)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Thrombospondin 1)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Brain/*metabolism
MH  - COS Cells
MH  - Chromatography, Affinity
MH  - Cloning, Molecular
MH  - Embryonic and Fetal Development
MH  - Gene Library
MH  - Hippocampus/metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/chemistry/*genetics/*metabolism
MH  - Neurons/*metabolism
MH  - Protein Sorting Signals/metabolism
MH  - Pyramidal Cells/metabolism
MH  - RNA, Messenger/genetics
MH  - Rats
MH  - Recombinant Proteins/biosynthesis/chemistry
MH  - Saccharomyces cerevisiae
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Thrombospondin 1/chemistry/genetics
MH  - Transcription, Genetic
MH  - Transfection
MH  - Tumor Cells, Cultured
EDAT- 1999/11/05 00:00
MHDA- 1999/11/05 00:01
CRDT- 1999/11/05 00:00
PHST- 1999/11/05 00:00 [pubmed]
PHST- 1999/11/05 00:01 [medline]
PHST- 1999/11/05 00:00 [entrez]
AID - 10.1006/bbrc.1999.1638 [doi]
AID - S0006-291X(99)91638-8 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1999 Nov;265(1):79-86. doi: 10.1006/bbrc.1999.1638.