Disease relevance of Crisp1

• Increased glomerular basement membrane permeability with loss of selectivity unrelated to changes in glomerular sialoprotein occurred with aging and was accompanied by increasing proteinuria [1].
• Degradation of pulmonary surfactant protein D by Pseudomonas aeruginosa elastase abrogates innate immune function [2].
• Reduced sialylation of podocalyxin--the major sialoprotein of the rat kidney glomerulus--in aminonucleoside nephrosis [3].
• Surfactant protein D (SP-D) gene-targeted mice develop severe pulmonary disease associated with emphysema, pulmonary lipidosis, and foamy macrophage infiltrations [4].
• The nonacylated form of protein D (PDm) of Haemophilus influenzae has been shown to induce the production of antibodies that are bactericidal to homologous and heterologous nontypeable H. influenzae (NTHi) strains [5].

Psychiatry related information on Crisp1

• When food intake is manipulated, but the dark-light cycle is unchanged, the circadian rhythm of SCP corresponds to feeding patterns and not light cycling [6].

High impact information on Crisp1

• Podocalyxin (PC), the major sialoprotein of glomerular epithelial cells (GECs), helps maintain the characteristic architecture of the foot processes and the patency of the filtration slits [7].
• Surfactant protein D interacts with Pneumocystis carinii and mediates organism adherence to alveolar macrophages [8].
• We have identified a major membrane sialoprotein in human glomeruli that is similar to rat podocalyxin in its sialic acid-dependent binding of wheat germ agglutinin and in its localization on the surface of glomerular epithelial and endothelial cells, as shown by immunoelectron microscopy, using the monoclonal antibody PHM5 [9].
• Endothelial cell membranes contain podocalyxin--the major sialoprotein of visceral glomerular epithelial cells [10].
• Podocalyxin is the major sialoprotein in the glycocalyx of glomerular podocytes [10].

Chemical compound and disease context of Crisp1

• The acylated form of protein D of Haemophilus influenzae is more immunogenic than the nonacylated form and elicits an adjuvant effect when it is used as a carrier conjugated to polyribosyl ribitol phosphate [5].
• Captopril treatment caused total regression of hypertension and LV hypertrophy and decreased both content and concentration of DNA and RNA, as well as the contents of MP, CP and SCP v the L -NAME group [11].
• A characterization of amiodarone-induced pulmonary toxicity in F344 rats and identification of surfactant protein-D as a potential biomarker for the development of the toxicity [12].

Biological context of Crisp1

• Amino acid sequence homology of AEG with metal-binding domains of several proteins suggests that AEG is a metalloprotein [13].
• Two classes of AEG cDNA, approximately 1500 base pairs (bp) and 950 bp in length, differed by 538 bp in the 3'-untranslated region and by four single nucleotide mismatches, one of which was in the coding region [13].
• Screening of a rat epididymal cDNA library with affinity-purified AEG antiserum yielded cDNA for AEG [13].
• Sterol carrier protein (SCP) is a highly abundant, ubiquitous, low molecular weight protein that has a rapid turnover and multifunctional roles in lipid metabolism and transport [14].
• The proliferative potential of cultured epididymal cells obtained from pubertal and old adult donors can be documented by [3H]thymidine labeling and mitotic indices without significant loss of gene expression for acidic epididymal glycoprotein [15].

Anatomical context of Crisp1

• Acidic epididymal glycoprotein (AEG) is a 31,000 molecular weight secretory protein of the rat epididymis [13].
• The level of sialoprotein present could not be due to contamination with serum or broken organelles [16].
• These findings strongly suggest that one of the functions of adrenal SCP is to participate in teh corticotropin-stimulated movement of cholesterol to the inner mitochondrial membrane for steroidogenesis [14].
• These and other characteristics led to studies on the possible role of SCP in mediation of steroidogenic responses of the adrenal gland to corticotropin [14].
• To quantitate the level of SCP in adrenal tissue and subcellular fractions, a specific immunochemical assay was developed using an antibody to homogeneous liver SCP [14].

Associations of Crisp1 with chemical compounds

• In vivo studies demonstrated that the level of total AEG mRNA is regulated by androgen [13].
• Low concentrations of deoxycholate and incubation in 0.25 M sucrose solution liberated a small amount of microsomal sialoprotein and this fraction exhibited a high degree of labeling of protein-bound N-acetylneuraminic acid [16].
• Other work showed mitochondrial SCP levels increase only in situations where there is an increase in cholesterol levels [14].
• The results show that the Arg-Gly-Asp sequence also confers cell-binding properties on bone-specific sialoprotein [17].
• When corticotropin was administered in vivo in the presence of aminoglutethimide, an inhibitor of steroidogenesis, there was a parallel movement of SCP with cholesterol to the inner mitochondrial membrane [14].

Other interactions of Crisp1

• Colocalization of dentin matrix protein 1 and dentin sialoprotein at late stages of rat molar development [18].
• The interdomain carbohydrate recognition domain-neck angle is significantly less in SP-A than in the homologous collectins, surfactant protein D, and mannose-binding protein [19].
• BACKGROUND: Loss of the cell membrane protein E-cadherin is a critical event during Ras-mediated transformation of intestinal epithelial cells [20].
• In marked contrast to the 5 alpha-reductase isozymes and proenkephalin, no significant age-related changes were observed in the mRNA levels for the androgen receptor, protein B/C, or protein D/E [21].
• As a preliminary to a study of the biogenesis of individual plasma membrane glycoproteins, the marker enzyme nucleotide pyrophosphatase (NPPase) and a major rat liver plasma membrane sialoprotein, subsequently found to be identical with the enzyme dipeptidyl peptidase IV (DPP IV), were purified 10,000- and 2,000-fold, respectively, from rat liver [22].

Analytical, diagnostic and therapeutic context of Crisp1

• Northern blot hybridization of epididymal RNA revealed two species of AEG mRNA, corresponding in length to each type of cDNA [13].
• Interactions of surfactant protein D with bacterial lipopolysaccharides. Surfactant protein D is an Escherichia coli-binding protein in bronchoalveolar lavage [23].
• A large number of cultured epididymal cells retain a differentiated function as demonstrated by the immunocytochemical and radioimmunoassay finding of acidic epididymal glycoprotein, a spermatozoa-coating protein secreted by the principal cells of rat epididymis [15].
• Immersion and perfusion of renal tissue with PEI reveals additional heavy staining of the epithelial and endothelial cell sialoprotein coatings [24].
• Then the sialoprotein was purified by high performance liquid chromatography from rat mandibulae using the monoclonal antibody as a marker [25].

References