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Caltrin

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https://www.readbyqxmd.com/read/27812283/structural-prediction-and-in-silico-physicochemical-characterization-for-mouse-caltrin-i-and-bovine-caltrin-proteins
#1
Ernesto J Grasso, Adolfo E Sottile, Carlos E Coronel
It is known that caltrin (calcium transport inhibitor) protein binds to sperm cells during ejaculation and inhibits extracellular Ca(2+) uptake. Although the sequence and some biological features of mouse caltrin I and bovine caltrin are known, their physicochemical properties and tertiary structure are mainly unknown. We predicted the 3D structures of mouse caltrin I and bovine caltrin by molecular homology modeling and threading. Surface electrostatic potentials and electric fields were calculated using the Poisson-Boltzmann equation...
2016: Bioinformatics and Biology Insights
https://www.readbyqxmd.com/read/26731031/no-obvious-phenotypic-abnormalities-in-mice-lacking-the-pate4-gene
#2
Timo Heckt, Johannes Keller, Roswitha Reusch, Kristin Hartmann, Susanne Krasemann, Irm Hermans-Borgmeyer, Michael Amling, Thorsten Schinke
We have previously reported that the hormone calcitonin (CT) negatively regulates bone formation by inhibiting the release of sphingosine-1-phosphate from bone-resorbing osteoclasts. In the context of this study we additionally observed that CT repressed the expression of Pate4, encoding the secreted protein caltrin/Svs7, in osteoclasts from wildtype mice. To assess a possible function of Pate4 in bone remodeling, we utilized commercially available embryonic stem cells with a targeted Pate4 allele to generate Pate4-deficient mice...
January 22, 2016: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/23590280/novel-inhibitory-activity-for-serine-protease-inhibitor-kazal-type-3-spink3-on-human-recombinant-kallikreins
#3
Diego Magno Assis, Lucia Zalazar, Maria Aparecida Juliano, Rosana De Castro, Andreina Cesari
Kallikrein-related peptidases (KLKs) are trypsin-like and chymotrypsin-like serine proteases which are expressed in several tissues. Their activity is tightly controlled by inhibitors including members of the serine protease Kazal-type (SPINK) family. These enzymes are promising targets for the treatment of skin desquamation, inflammation and cancer. Spink3 or caltrin I is expressed in mouse pancreas and males accessory glands and the resulting mature protein has been associated with different activities such as an inhibitor of trypsin and acrosin activity, calcium transport inhibitor in sperm and inhibitor of cell proliferation during embryogenesis...
October 2013: Protein and Peptide Letters
https://www.readbyqxmd.com/read/22228629/spink3-modulates-mouse-sperm-physiology-through-the-reduction-of-nitric-oxide-level-independently-of-its-trypsin-inhibitory-activity
#4
L Zalazar, T E Saez Lancellotti, M Clementi, C Lombardo, L Lamattina, R De Castro, M W Fornés, A Cesari
Serine protease inhibitor Kazal-type (SPINK3)/P12/PSTI-II is a small secretory protein from mouse seminal vesicle which contains a KAZAL domain and shows calcium (Ca(2+))-transport inhibitory (caltrin) activity. This molecule was obtained as a recombinant protein and its effect on capacitated sperm cells was examined. SPINK3 inhibited trypsin activity in vitro while the fusion protein GST-SPINK3 had no effect on this enzyme activity. The inactive GST-SPINK3 significantly reduced the percentage of spermatozoa positively stained for nitric oxide (NO) with the specific probe DAF-FM DA and NO concentration measured by Griess method in capacitated mouse sperm; the same effect was observed when sperm were capacitated under low Ca(2+) concentration, using either intracellular (BAPTA-AM) or extracellular Ca(2+) (EDTA) chelators...
March 2012: Reproduction: the Official Journal of the Society for the Study of Fertility
https://www.readbyqxmd.com/read/18718917/adaptive-evolution-in-rodent-seminal-vesicle-secretion-proteins
#5
Robert C Karn, Nathaniel L Clark, Eric D Nguyen, Willie J Swanson
Proteins involved in reproductive fitness have evolved unusually rapidly across diverse groups of organisms. These reproductive proteins show unusually high rates of amino acid substitutions, suggesting that the proteins have been subject to positive selection. We sought to identify seminal fluid proteins experiencing adaptive evolution because such proteins are often involved in sperm competition, host immunity to pathogens, and manipulation of female reproductive physiology and behavior. We performed an evolutionary screen of the mouse prostate transcriptome for genes with elevated evolutionary rates between mouse and rat...
November 2008: Molecular Biology and Evolution
https://www.readbyqxmd.com/read/18550793/rat-caltrin-protein-modulates-the-acrosomal-exocytosis-during-sperm-capacitation
#6
Andrea Dematteis, Sabrina D Miranda, Maria L Novella, Cristina Maldonado, Ruben H Ponce, Julieta A Maldera, Patricia S Cuasnicu, Carlos E Coronel
Caltrin is a small and basic protein of the seminal vesicle secretion that inhibits sperm calcium uptake. The influence of rat caltrin on sperm physiological processes related to fertilizing competence was studied by examining its effect on 1) spontaneous acrosomal exocytosis, 2) protein tyrosine phosphorylation, and 3) sperm-egg interaction. Results show that the presence of caltrin during in vitro capacitation both reduced the rate of spontaneous acrosomal exocytosis without altering the pattern of protein tyrosine phosphorylation, and enhanced the sperm ability to bind to the zona pellucida (ZP)...
September 2008: Biology of Reproduction
https://www.readbyqxmd.com/read/18430598/isolation-characterization-and-cdna-sequencing-of-a-kazal-family-proteinase-inhibitor-from-seminal-plasma-of-turkey-meleagris-gallopavo
#7
Mariola Słowińska, Mariusz Olczak, Mariola Wojtczak, Jan Glogowski, Jan Jankowski, Wiesław Watorek, Ryszard Amarowicz, Andrzej Ciereszko
The turkey reproductive tract and seminal plasma contain a serine proteinase inhibitor that seems to be unique for the reproductive tract. Our experimental objective was to isolate, characterize and cDNA sequence the Kazal family proteinase inhibitor from turkey seminal plasma and testis. Seminal plasma contains two forms of a Kazal family inhibitor: virgin (Ia) represented by an inhibitor of moderate electrophoretic migration rate (present also in the testis) and modified (Ib, a split peptide bond) represented by an inhibitor with a fast migration rate...
June 2008: Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology
https://www.readbyqxmd.com/read/15240421/androgen-dependent-expression-gene-structure-and-molecular-evolution-of-guinea-pig-caltrin-ii-a-wap-motif-protein
#8
Yutaka Furutani, Akira Kato, Ryoji Kawai, Azzania Fibriani, Soichi Kojima, Shigehisa Hirose
We determined the cDNA and gene structures of guinea pig caltrin II, a unique member of the calcium transporter inhibitors containing a whey acidic protein (WAP) motif, and we established that it is a secretory protein with a potential 21-amino acid signal peptide in its N-terminus. Northern blot analysis and in situ hybridization histochemistry indicated that the expression of caltrin II is restricted to luminal epithelial cells in the seminal vesicles. Its message levels markedly decreased either after castration (and were restored by simultaneous administration of testosterone) or after treatment of the animals with estradiol, suggesting that the expression of caltrin II is androgen-dependent...
November 2004: Biology of Reproduction
https://www.readbyqxmd.com/read/12767821/expression-of-caltrin-in-the-baculovirus-system-and-its-purification-in-high-yield-and-purity-by-cobalt-ii-affinity-chromatography
#9
COMPARATIVE STUDY
Tony C A Phan, Kristen J Nowak, P Anthony Akkari, Ming H Zheng, Jiake Xu
Direct protein extraction from animals is the only approach available to obtain caltrin, calcium transport inhibitor. Here we report the expression and purification of caltrin, previously shown to hinder the influx of calcium into epididymal spermatozoa. Cloning of the caltrin gene into the pCDNA3.1 V5/His-TOPO vector and the subsequent ligation of the caltrin-His sequence into the transfer vector pBacPAK9 allowed the expression of recombinant caltrin using the baculovirus expression vector system (BEVS). Recombinant His-tagged caltrin was purified utilising both nickel (II)-nitrilotriacetic acid (Ni(2+)-NTA) and cobalt (II)-carboxymethylaspartate (Co(2+)-CmAsp) immobilised metal affinity chromatography (IMAC)...
June 2003: Protein Expression and Purification
https://www.readbyqxmd.com/read/11840564/the-characterisation-of-novel-secreted-ly-6-proteins-from-rat-urine-by-the-combined-use-of-two-dimensional-gel-electrophoresis-microbore-high-performance-liquid-chromatography-and-expressed-sequence-tag-data
#10
Christopher Southan, Paul Cutler, Helen Birrell, John Connell, Kenneth G M Fantom, Matthew Sims, Narjis Shaikh, Klaus Schneider
A proteomic study of rat urine was undertaken using two-dimensional gel electrophoresis, microbore high performance liquid chromatography, mass spectrometry and N-terminal sequencing. Five known urinary proteins were identified but two novel peptide fragments matched a large number of rat expressed sequence tags (ESTs) from a liver library. By combining protein chemical and nucleotide data, two 101-residue open reading frames with 90% amino acid identity were determined, rat urinary protein 1 (RUP-1) and RUP-2...
February 2002: Proteomics
https://www.readbyqxmd.com/read/11330645/regulation-of-caltrin-mrna-expression-by-androgens-in-the-murine-prostate
#11
J Mirosevich, J M Bentel, J S Dawkins
Testicular androgens induce the proliferation and differentiation of prostatic epithelial cells by regulating the expression of androgen target genes. The use of subtractive hybridization to isolate genes that are differentially expressed during the early phase of androgen-induced prostatic regrowth in castrated mice resulted in identification of the murine caltrin gene. Caltrin messenger RNA (mRNA) was highly expressed in the prostates of intact mice. Five weeks following castration of mice, steady state caltrin mRNA levels were reduced by 70%...
May 2001: Journal of Andrology
https://www.readbyqxmd.com/read/10859240/trypsin-acrosin-inhibitor-activity-of-rat-and-guinea-pig-caltrin-proteins-structural-and-functional-studies
#12
D E Winnica, M L Novella, A Dematteis, C E Coronel
Dramatic inhibition of trypsin activity by rat caltrin and guinea pig caltrin I was spectrophotometrically demonstrated using the artificial substrate benzoylarginyl ethyl ester. Approximately 6% and 21% of residual proteolytic activity was recorded after preincubating the enzyme with 0.22 and 0.27 microM rat caltrin and guinea pig caltrin I, respectively. Reduction and carboxymethylation of the cysteine residues abolished the inhibitor activity of both caltrin proteins. Rat caltrin and guinea pig caltrin I show structural homology with secretory trypsin/acrosin inhibitor proteins isolated from boar and human seminal plasma and mouse seminal vesicle secretion and share a fragment of 13 amino acids of almost identical sequence (DPVCGTDGH/K/ITYG/AN), which is also present in the structure of Kazal-type trypsin inhibitor proteins from different mammalian tissues...
July 2000: Biology of Reproduction
https://www.readbyqxmd.com/read/10445100/androgen-dependent-synthesis-secretion-of-caltrin-calcium-transport-inhibitor-protein-of-mammalian-seminal-vesicle
#13
M L Novella, C Maldonado, A Aoki, C E Coronel
Effects of androgen status on the synthesis and secretion of rat caltrin have been studied by three different procedures: a) immunocytochemistry in seminal vesicle tissues; b) polyacrylamide gel electrophoresis and Western immunostaining of seminal vesicle secretion; and c) evaluation of trypsin inhibitory activity of the seminal vesicle secretion. Rat caltrin has been immunolocalized in cells of the secretory epithelium, specifically in the electron-lucent halo of secretory granules which store and transport proteins to the lumen...
July 1999: Archives of Andrology
https://www.readbyqxmd.com/read/10232662/rat-seminal-vesicle-secretory-protein-svs-ii-binds-dna-with-a-preference-for-the-5-regulatory-region-of-secretory-protein-svs-iv-gene-co-isolation-with-components-of-the-nuclear-matrix
#14
M J Horton, R H Getzenberg
In rats, the ventral prostate and seminal vesicles produce distinct sets of proteins whose functions and tissue-specific regulation by androgens remain unclear. We have utilized the genes encoding the major secretory protein of seminal vesicles, SVS IV, and the C3 subunit of prostatein of the ventral prostate to study how the nuclear matrix might determine their tissue-specific gene expression. Nuclear matrix proteins were prepared from purified nuclei with DNase and 2 M NaCl, separated in SDS gels, and transferred onto membranes for DNA-binding (southwestern) and immunological (western) analyses...
March 1999: Journal of Andrology
https://www.readbyqxmd.com/read/9828198/developmental-profile-of-a-caltrin-like-protease-inhibitor-p12-in-mouse-seminal-vesicle-and-characterization-of-its-binding-sites-on-sperm-surface
#15
L Y Chen, Y H Lin, M L Lai, Y H Chen
We examined the developmental profile of a kazal-type trypsin inhibitor (P12) of Mr 6126 in mouse seminal vesicle, characterized its binding sites on the surface of sperm, and assessed its effect on Ca2+ uptake by spermatozoa. Among the genital tracts of adult mice, P12 was found only in the male accessory glands including seminal vesicle, coagulating gland, and prostate. It was immunolocalized on the luminal epithelium of the primary and secondary folds in both the seminal vesicle and coagulating gland, and on the folds projecting into the lumen of the glandular alveolus in the prostate...
December 1998: Biology of Reproduction
https://www.readbyqxmd.com/read/9009216/identification-of-the-region-that-plays-an-important-role-in-determining-antibacterial-activity-of-bovine-seminalplasmin
#16
N Sitaram, C Subbalakshmi, V Krishnakumari, R Nagaraj
Seminalplasmin (SPLN) is a 47-residue protein isolated from bovine seminal plasma having potent antimicrobial activity against a broad spectrum of microorganisms. SPLN, also known as caltrin, acts as a calcium transport regulator in bovine sperms. Analysis of the sequence of SPLN reveals a 27-residue stretch with the sequence SLSRYAKLANRLANPKLLETFLSKWIG more hydrophobic than the rest of the protein. It is demonstrated that a synthetic peptide corresponding to this 27-residue segment has antimicrobial activity comparable to that of SPLN...
January 6, 1997: FEBS Letters
https://www.readbyqxmd.com/read/8585779/electron-microscopic-immunolocalization-of-caltrin-proteins-in-guinea-pig-seminal-vesicles
#17
C E Coronel, C Maldonado, A Aoki, H A Lardy
Caltrins, the small, basic proteins of the seminal vesicle secretion that inhibit calcium transport into epididymal spermatozoa, and consequently the onset of the acrosome reaction and the hyperactivated motility, were localized in the epithelial cells and the lumen of the seminal vesicles of the guinea pig by an immunocytochemical procedure and electron microscopy. Rabbit antisera against each protein (caltrin I or II), and goat anti-rabbit IgG antiserum labeled with colloidal gold were used to detect the caltrin immunoreaction...
November 1995: Archives of Andrology
https://www.readbyqxmd.com/read/8444904/caltrin-the-calcium-transport-regulatory-peptide-of-spermatozoa-modulates-acrosomal-exocytosis-in-response-to-the-egg-s-zona-pellucida
#18
E N Clark, M E Corron, H M Florman
Acrosomal exocytosis is initiated in mammalian sperm by stimulatory agonists in the zona pellucida. Recently, it was shown that exocytosis is modulated in bovine sperm by extrinsic factors present in seminal fluids (Florman, H.M., and First, N.L. (1988) Dev. Biol. 128, 464-474). Fractionation of bovine seminal fluids yields a M(r) approximately 6,500, basic (pI approximately 8.5) peptide that accounts for the positive modulation of zona pellucida-induced acrosome reaction (ED50 and maximal response at 0.2 and 1 micrograms/ml, respectively)...
March 5, 1993: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/8318586/isolation-and-characterization-of-a-54-kilodalton-precursor-of-caltrin-the-calcium-transport-inhibitor-protein-from-seminal-vesicles-of-the-rat
#19
C E Coronel, M L Novella, D E Winnica, H A Lardy
A basic 54-kDa protein (pI approximately 8.8) that cross-reacts with anti-caltrin antisera has been detected and isolated by gel filtration and cation exchange chromatography from seminal vesicle content of the rat. The soluble protein spontaneously precipitated in NaHCO3-buffered solution at pH 7.8, but it was kept soluble in imidazole buffer containing EDTA and dithiothreitol at pH 7.0. In addition to the main band of 54 kDa, two faint immunoreactive fractions with molecular weights around 45,000 and 14,000 were also revealed by Western blotting...
June 1993: Biology of Reproduction
https://www.readbyqxmd.com/read/8218634/lysogenic-activity-of-enhancer-caltrin-and-the-influence-of-phospholipids-on-its-expression
#20
J T San Agustin, H A Lardy
Enhancer caltrin permeabilizes the plasma membrane of bovine epididymal spermatozoa as indicated by the release of hyaluronidase from the acrosome and lactate dehydrogenase (LDH) from the sperm cytosol. A previously reported increased calcium uptake by the sperm in the presence of enhancer caltrin was apparently due, in part, to calcium entry into the mitochondria, which had become accessible to external calcium. At 37 microM (200 micrograms/ml), enhancer caltrin released about 30% of the total hyaluronidase in the acrosome and 50% of the cytosolic LDH from epididymal sperm (4 x 10(7)/ml)...
October 1993: Biology of Reproduction
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