Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:Q9UIJ5 (Rec)
 58,342 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The cause of the increased egg weight in hens with lathyrism was investigated by feeding laying birds with diets containing beta-aminopropionitrile, the toxic principle of certain legume seeds in the genus Lathyrus. There was a significant increase (P less than 0.01) in the amount of albumen in the egg owing to an increased formation of thin white. The water permeability of the shell membranes demonstrated an increased porosity and a loss of tensile strength which contributed not only to a high water uptake but also to abnormalities of the shape of eggs during 'plumping'. It was concluded that a defect in the shell membrane protein system alters the membrane's general properties and that the increased egg weight in lathyrism is a result of the defect.
Vet Rec 1988 Sep 03
PMID:Lathyrism in laying hens and increases in egg weight. 318 49

The major outer membrane protein (P2) of Haemophilus influenzae type b (Hib) with an apparent molecular weight of 37,000 to 40,000 has been previously shown to function as a porin and also as a target for antibodies protective against experimental Hib disease. The gene encoding the Hib P2 protein was cloned by using a shuttle vector capable of replication in both Escherichia coli and H. influenzae. The amino acid sequence of the amino terminus of the Hib P2 protein was determined and used to design an oligonucleotide probe corresponding to the first 20 amino acids of this protein. This oligonucleotide probe was used to identify Hib chromosomal DNA fragments containing the Hib P2 gene. These DNA fragments were ligated into the plasmid vector pGJB103 and then used to transform a rec-1 mutant of H. influenzae Rd. Recombinant clones expressing the Hib P2 protein were identified in a colony blot-radioimmunoassay by using a monoclonal antibody specific for a surface epitope of the Hib P2 protein. The gene encoding this Hib protein was present on a 10-kilobase Hib DNA insert in the recombinant plasmid. Transformation experiments involving the recombinant plasmid suggested that unregulated synthesis of Hib P2 is a lethal event in E. coli. The recombinant Hib P2 protein was exposed on the surface of the recombinant H. influenzae strain. This recombinant strain was used to develop a system for detecting polyclonal serum antibodies directed against surface determinants of the Hib P2 protein. The availability of the gene encoding the Hib P2 protein should facilitate investigation of both the immunogenicity and the structure-function relationship(s) of this major outer membrane protein.
 ...
PMID:Cloning of the gene encoding the major outer membrane protein of Haemophilus influenzae type b. 326 90

In search of unique components of the seminiferous tubule extracellular matrix, monoclonal antibodies were raised against an isolated seminiferous tubule extracellular matrix, and the monoclonal antibody 12G11 was cloned. By immunofluorescence microscopy in eight kinds of rat tissues (testis, lung, liver, small intestine, cardiac muscle, skeletal muscle, kidney, and brain), 12G11 antigen existed only in the testis. Immunoelectron microscopy revealed that the antigen is localized in the basement membrane of the seminiferous tubule and in the basement membranes of myoid cells. For a biochemical analysis, eight kinds of rat extracellular matrices were isolated and solubilized with 8 M urea and 2% beta-mercaptoethanol. Immunoblot analysis of these samples in 0.8% agarose gel also showed that the antigen was specific for the testis, and in a two high-molecular weight aggregates. These aggregates seemed to contain type IV collagen and laminin chains. The antigen of 12G11 antibody was shown to be 27 kDa by 10% SDS-PAGE followed by immunoblotting. From these data, the existence of a testis specific 27 kDa basement membrane protein, which associate with type IV collagen and laminin, was suggested.
Anat Rec 2000 12 01
PMID:27 kDa extracellular matrix protein revealed by a monoclonal antibody raised against rat testis. 1107 6

Hepatitis C virus (HCV), which is the major pathogen responsible for human chronic liver disease, has special tropism for hepatocytes. Although, low-density lipoprotein receptor, CD81 and negatively charged glycosaminoglycans have been proposed as candidate receptors for HCV, no confirmed receptor(s) on the hepatocytes have been identified to date. It is also suggested that additional, yet unidentified, cellular proteins may be involved in the host-viral interaction. Therefore, this study was conducted with the main aim to identify hepatocyte protein(s) that may have affinity for the HCV structural protein, envelope-2/non-structural-1 (E2/NS1) protein. For the binding studies, hepatocytes were isolated from fresh normal human liver tissues. The hepatocyte proteins on the nitrocellulose paper were reacted with recombinant E2/NS1 protein and anti-E2 (rabbit). In another approach, to rule out the possibility of binding of rec-E2/NS1 with the hepatocyte cytoplasmic proteins, hepatocyte plasma membrane proteins were passed through CNBr-activated and recombinant E2/NS1 bound sepharose-4B column. The recombinant E2/NS1 binding hepatocyte plasma membrane protein(s) were eluted and were then analyzed. Altogether, our data suggest that E2/NS1 protein of HCV binds to two hepatocyte proteins of molecular weights 25-28 kDa and 59-60 kDa. These results indicate the possible role of the above proteins (25-28 kDa and 59-60 kDa) in the viral binding to the hepatocytes.
 ...
PMID:Identification of human hepatocyte protein(s), which binds specifically to the recombinant envelope-2/non-structural-1 protein of hepatitis C virus. 1219 77

Thirty-five isolates of Pasteurella multocida from the vagina and respiratory tract of sheep were compared by analysing their capsular polysaccharide types and outer membrane protein profiles. The phylogenetic relationships of selected isolates with respect to reference strains of P. multocida were also determined by comparative 16S rRNA sequence analysis. Three capsular types, A, D and F, and three major outer membrane protein types were identified, and there were four different combinations of these characteristics which probably marked four individual clones of P. multocida. Strains representing three of these clones were recovered from cases of ovine pneumonia, whereas isolates of the fourth clone were associated exclusively with the vagina of healthy ewes and the liver of a dead septicaemic lamb on the same farm. Analysis of the 16S rRNA sequences showed that there was 100 per cent identity between representative pneumonic isolates and reference strains of P. multocida subspecies galliseptica and P. multocida subspecies multocida. The 16S rRNA genes of representative vaginal and liver isolates from the same farm were identical but differed from the other strains at one nucleotide position, providing strong evidence that the vaginal and liver isolates represent a distinct subpopulation of P. multocida.
Vet Rec 2003 Jan 04
PMID:Comparative analyses of Pasteurella multocida strains associated with the ovine respiratory and vaginal tracts. 1254 66

Skin is an important region of somatic sensory input, and is one of the most innervated areas of the human body. In this study, we investigated in human hand skin the distribution of nervous structures immunoreactive for the growth-associated protein 43 (GAP-43) and the protein gene product 9.5 (PGP 9.5). GAP-43 is a neuronal presynaptic membrane protein that is generally considered to be a marker of neuronal plasticity. PGP 9.5 is a neuron-specific soluble protein that is widely used as general marker for the peripheral nervous system. The entire neural network of the dermis and epidermis was stained with antibody to PGP 9.5. In the dermis, there were fewer GAP-43-immunostained nerve fibers than PGP 9.5-immunostained nerve fibers, whereas in the epidermis the numbers were equal. Only some Merkel cells and Meissner corpuscles were GAP-43-immunoreactive. In conclusion, our results show that GAP-43 protein is expressed in a subset of PGP 9.5-immunoreactive nerve structures.
Anat Rec A Discov Mol Cell Evol Biol 2003 May
PMID:Distribution of GAP-43 nerve fibers in the skin of the adult human hand. 1270 5

X-linked Emery-Dreifuss muscular dystrophy (X-EDMD) is inherited through mutations in EMD, which encodes a nuclear membrane protein named emerin. Emerin is expressed in most cells, but EDMD strikes specific tissues. This review summarizes growing evidence that emerin has roles in both tissue-specific gene regulation and the mechanical integrity of the nucleus and discusses how these roles might impact EDMD.
Anat Rec A Discov Mol Cell Evol Biol 2006 Jul
PMID:Multiple roles for emerin: implications for Emery-Dreifuss muscular dystrophy. 1676 Dec 79

The laminin alpha1 chain is a subunit of laminin-1, a heterotrimeric basement membrane protein. The LG4-5 module at the C terminus of laminin alpha1 contains major binding sites for heparin, sulfatide, and alpha-dystroglycan and plays a critical role in early embryonic development. We previously identified active synthetic peptides AG73 and EF-1 from the sequence of laminin alpha1 LG4 for binding to syndecan and integrin alpha2beta1, respectively. However, their activity and functional relationship within the laminin-1 and LG4 as well as the functional relation between these sites and alpha-dystroglycan binding sites in LG4 are not clear. To address these questions, we created mutant recombinant LG4 proteins containing alanine substitutions within the AG73 (M1), EF-1 (M2, M3), and alpha-dystroglycan binding sites (M4, M5) and analyzed their activities. We found that recombinant proteins rec-M1 and rec-M5, containing mutations within M1 and M5, respectively, did not bind heparin or lymphoid cell lines expressing syndecans. These results suggest that LG4 binds to heparin and syndecans through M1 and M5. Rec-M1 and rec-M5 reduced fibroblast attachment, whereas mutant rec-M2 and rec-M3 retained cell attachment activity but did not promote cell spreading. Fibroblast attachment to rec-LG4 was inhibited by heparin but not by integrin antibodies. Spreading of fibroblasts on rec-LG4 was inhibited by anti-integrin alpha2 and beta1 but not by anti-integrin alpha1 and alpha6. These results suggest that the M1 and M5 sites are necessary for cell attachment on LG4 through syndecans and that the EF-1 site is for cell spreading activity through integrin alpha2beta1. In contrast, laminin-1-mediated fibroblast attachment and spreading were not inhibited by heparin or anti-integrin alpha2. Our findings indicate that LG4 has a unique function distinct from laminin-1 and suggest that laminin alpha1 LG4-5 may also be produced by a proteolytic cleavage in certain tissues where it exerts its activity.
 ...
PMID:Laminin alpha1 chain LG4 module promotes cell attachment through syndecans and cell spreading through integrin alpha2beta1. 1694 29

Squirrels are highly visual mammals with an expanded cortical visual system and a number of well-differentiated architectonic fields. To describe and delimit cortical fields, subdivisions of cortex were reconstructed from serial brain sections cut in the coronal, sagittal, or horizontal planes. Architectonic characteristics of cortical areas were visualized after brain sections were processed with immunohistochemical and histochemical procedures for revealing parvalbumin, calbindin, neurofilament protein, vesicle glutamate transporter 2, limbic-associated membrane protein, synaptic zinc, cytochrome oxidase, myelin or Nissl substance. In general, these different procedures revealed similar boundaries between areas, suggesting that functionally relevant borders were being detected. The results allowed a more precise demarcation of previously identified areas as well as the identification of areas that had not been previously described. Primary sensory cortical areas were characterized by sparse zinc staining of layer 4, as thalamocortical terminations lack zinc, as well as by layer 4 terminations rich in parvalbumin and vesicle glutamate transporter 2. Primary areas also expressed higher levels of cytochrome oxidase and myelin. Primary motor cortex was associated with large SMI-32 labeled pyramidal cells in layers 3 and 5. Our proposed organization of cortex in gray squirrels includes both similarities and differences to the proposed of cortex in other rodents such as mice and rats. The presence of a number of well-differentiated cortical areas in squirrels may serve as a guide to the identification of homologous fields in other rodents, as well as a useful guide in further studies of cortical organization and function.
Anat Rec (Hoboken) 2008 Oct
PMID:Architectonic subdivisions of neocortex in the gray squirrel (Sciurus carolinensis). 1878 Feb 99

Distribution of three soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE) proteins, syntaxin-1, synaptosomal-associated protein of 25 kDa (SNAP-25), and vesicle-associated membrane protein-2 (VAMP-2), was examined in dental pulp and periodontal ligament of the rat incisor. In the trigeminal ganglion, syntaxin-1 and SNAP-25 immunoreactivity was predominately detected in medium- to large-sized neurons. Most syntaxin-1 immunoreactive neurons expressed SNAP-25. In contrast, VAMP-2 was localized in small- to medium-sized neurons and in slender-shaped cells surrounding SNAP-25-immunopositive neurons. When the inferior alveolar nerve, one of the mandibular nerve branches innervating the dental pulp and periodontal ligament, was ligated, SNARE proteins accumulated at the site proximal to the ligation. In the incisor dental pulp, all nerve fibers displayed immunoreactivity for syntaxin-1, SNAP-25, and VAMP-2. In the periodontal ligament of the incisor, almost all nerve fibers displayed both syntaxin-1 and SNAP-25 immunoreactivity, but lacked VAMP-2 immunoreactivity. SNAP-25 protein expression was localized around the vesicle membranes at the axon terminal of the periodontal mechanoreceptors. These present data suggest that these three SNARE proteins are synthesized at the trigeminal ganglion, transported centrally and peripherally, and expressed in sensory endings where apparent synapses are not present. Because those proteins participate in docking and exocytosis of synapse vesicles in the central nervous system, they might also contribute to vesicle exocytosis at receptive fields where apparent synapses are not present.
Anat Rec (Hoboken) 2010 Jun
PMID:Immunohistochemical localization of SNARE proteins in dental pulp and periodontal ligament of the rat incisor. 2018 59


1 2 Next >>