The amino acid sequence of neuropolypeptide h3 from Homo sapiens brain has been determined. It revealed that h3 is the exact counterpart of the 21-kDa protein from Bos taurus brain and the 23-kDa protein from Rattus norvegicus brain: The three proteins belong to the same 21-23-kDa protein family. Multiple tissue Northern blots showed that the mRNA encoding the 21-23-kDa protein is expressed in different amounts according to tissues and species; it is particularly abundant in Rattus norvegicus testis.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1007/BF00160411 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Comparative Characterization of Four Calcium-Binding EF Hand Proteins from .
Korean J Parasitol
February 2018
Graduate Program in Biomedical Sciences, Faculty of Allied Health Sciences, Thammasat University, Pathumthani 12120, Thailand.
Four isoforms of calcium binding proteins containing 2 EF hand motifs and a dynein light chain-like domain in the human liver fluke , namely OvCaBP1, 2, 3, and 4, were characterized. They had molecular weights of 22.7, 21.
View Article and Find Full Text PDFExpression of caveolin-1 in the interfollicular but not the follicle-associated epithelial cells in the bursa of fabricius of chickens.
J Morphol
January 2018
Department of Anatomy Histology and Embryology, Semmelweis University, Budapest, 1094, Hungary.
The surface epithelium of the bursa of Fabricius consists of interfollicular (IFE) and follicle-associated epithelium (FAE). The IFE comprises (i) cylindrical-shaped secretory cells (SC) and (ii) cuboidal basal cells (BCs). The FAE provides histological and two-way functional connections between the bursal lumen and medulla of the follicle.
View Article and Find Full Text PDFCCBE1 enhances lymphangiogenesis via A disintegrin and metalloprotease with thrombospondin motifs-3-mediated vascular endothelial growth factor-C activation.
Circulation
May 2014
Wihuri Research Institute (M.J., A.A., V.-M.L., R.K., K.A.), Translational Cancer Biology Program (M.J., S.K.J., D.T., A.A., T.H., K.A.), and Department of Biomedicine (M.J.), Biomedicum Helsinki, University of Helsinki, Helsinki, Finland; Biotechnology Programme, Spanish National Cancer Research Centre, Madrid, Spain (S.O.); Hubrecht Institute, Utrecht, The Netherlands (T.K.); and Helsinki University Central Hospital, Helsinki, Finland (K.A.).
Background: Hennekam lymphangiectasia-lymphedema syndrome (Online Mendelian Inheritance in Man 235510) is a rare autosomal recessive disease, which is associated with mutations in the CCBE1 gene. Because of the striking phenotypic similarity of embryos lacking either the Ccbe1 gene or the lymphangiogenic growth factor Vegfc gene, we searched for collagen- and calcium-binding epidermal growth factor domains 1 (CCBE1) interactions with the vascular endothelial growth factor-C (VEGF-C) growth factor signaling pathway, which is critical in embryonic and adult lymphangiogenesis.
Methods And Results: By analyzing VEGF-C produced by CCBE1-transfected cells, we found that, whereas CCBE1 itself does not process VEGF-C, it promotes proteolytic cleavage of the otherwise poorly active 29/31-kDa form of VEGF-C by the A disintegrin and metalloprotease with thrombospondin motifs-3 protease, resulting in the mature 21/23-kDa form of VEGF-C, which induces increased VEGF-C receptor signaling.
Serological diagnosis of North American Paragonimiasis by Western blot using Paragonimus kellicotti adult worm antigen.
Am J Trop Med Hyg
June 2013
Infectious Diseases Division, Department of Internal Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA.
Abstract. We studied the value of an IgG Western blot (WB) with Paragonimus kellicotti (Pk) antigen for diagnosis of North American paragonimiasis. The test was evaluated with sera from patients with Pk and Paragonimus westermani infections, with control sera from patients with other helminth infections, and sera from healthy Americans.
View Article and Find Full Text PDFMolecular characterization and NF-κB-regulated transcription of selenoprotein S from the Bama mini-pig.
Mol Biol Rep
October 2011
The State Key Laboratory for Animal Nutrition, Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100193, People's Republic of China.
Selenoprotein S (SelS), a member of selenoprotein family, plays important regulatory function in inflammation and metabolic diseases. SelS expression is up-regulated response to the inflammatory stimulus in many mammal cells, animal models as well as patients. In order to further understand the function of SelS gene, molecular characterization and transcriptional regulation of SelS from a Bama mini-pig were analyzed in the present study.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!