Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01178 (oxytocin)
 15,767 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The objectives of the present study were 1) to determine the heterogeneity of the MAC-T cell line; 2) to examine whether homogeneous clones could be derived from MAC-T cells; and 3) to examine cell morphology, cytoskeletal characteristics, size, colony-forming ability, growth characteristics, beta-casein production, response to oxytocin, and cytogenetic properties of the clones. Three clonal cells, designated CU-1, CU-2, and CU-3, were derived from MAC-T cells. CU-1 and CU-2 cells were morphologically homogeneous. CU-3 cells were heterogeneous and contained two distinct subtypes. All clones contained cytokeratin 14 and 18. CU-2 and CU-3 cells were 30 and 18% larger, respectively, than CU-1 cells. CU-1 cells did not grow in serum-free medium. Doubling times for MAC-T, CU-2, and CU-3 were 46, 48, and 78 h, respectively, in serum-free medium. MAC-T cells and clones constitutively expressed beta-casein in culture ranging from .1 to .3 micrograms/ml per 24 h. Cytogenetic analyses revealed Robertsonian translocations and isochromosomes in the clonal lines. We conclude that parental MAC-T cells are heterogeneous in morphology, growth, and cytogenetic characteristics.
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PMID:Subcloning the MAC-T bovine mammary epithelial cell line: morphology, growth properties, and cytogenetic analysis of clonal cells. 754 Jan 86

The objectives of the study were to purify porcine beta-casein from sow's milk, to determine N-terminal amino acid sequence, to develop specific antisera against porcine beta-casein, and to use that antisera to evaluate milk samples from a mastitis study. Milk was collected by hand milking a Yorkshire by Duroc crossbred sow following oxytocin administration on d 27 of lactation. A casein-enriched fraction was then prepared by iso-electric precipitation. Porcine beta-casein was then purified by liquid chromatography on a Mono Q anion-exchange column, and checked for purity with SDS-PAGE. An apparent molecular weight of 29,000 Da was estimated from SDS-PAGE. N-Terminal amino acid sequence was determined by Edman degradation to be RAKEELNASGETVE. Rabbits (n = 2) were immunized with beta-casein mixed with Freund's complete (primary) or incomplete (boosters) adjuvant at 4-wk intervals. Antiserum collected from one rabbit 112 d after primary immunization detected 30 to 100 ng beta-casein by Western blot procedure when used at a dilution of 1:2 x 10(6). The antiserum was specific for porcine beta-casein, but showed some cross-reactivity with equine casein. It was determined by Western blot procedure that mammary inflammation induced by lipopolysaccharide infusion resulted in a 41% decrease in the beta-casein concentration of sow milk.
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PMID:Purification of porcine beta-casein, N-terminal sequence, quantification in mastitic milk. 1216 53

In the work described in this article, mouse fetal fibroblasts were treated with three lactation hormones (insulin, progesterone and oxytocin) and the cellular changes were analyzed by RT-PCR-Southern hybridization. A gene-expression pattern characteristic of mammary epithelioid cells was induced by the hormones, as indicated by expression of the marker genes alpha-casein and beta-casein. Two mammary epithelial cell-specific gene expression vectors were constructed with bovine alpha-s1-casein or ovine beta-casein gene promoters directing an EGFP reporter gene. Transient expression of the EGFP gene was observed in cells treated by the hormones but not in control cells. Cell morphology also changed after insulin and oxytocin treatments; the cells resembled epithelial cells rather than fibroblasts. Our results suggest that mouse fetus fibroblasts can be partially induced by lactation hormones to resemble mammary epithelial cells. This procedure might help to increase the efficiency of gene targeting in studies of mammary gland bioreactors.
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PMID:Plasticity of the response of fetal mouse fibroblast to lactation hormones. 1297 81

Normal development of the mammary gland is fundamental for lactation and requires exquisite cellular coordination. The gap junction proteins Cx26, Cx32 and Cx30 have been reported in luminal epithelial cells of the mammary gland while Cx43 is expressed in myoepithelial cells and in the stroma. This project aimed to determine the role of Cx43 in mammary gland development and function by employing a mouse model (Gja1(Jrt/+)) that harbors an autosomal dominant Cx43 mutation, and wild-type (WT) littermates. The highly phosphorylated species of Cx43, the total gap junction plaque number and gap junctional intercellular communication were reduced in mammary glands from Gja1(Jrt/+) mice, resulting in delayed development of the ducts. At parturition, Cx43 levels and gap junction plaque numbers were still reduced in Gja1(Jrt/+) mice, yet the morphology of the gland did not differ from WT mice. Interestingly, while higher than WT levels of beta-casein and WAP were present in the gland of Gja1(Jrt/+) mice, oxytocin failed to stimulate milk delivery to the ducts. Together, these data revealed that decreased levels of Cx43 result in delayed development of the mammary gland and a full complement of Cx43 is necessary for the expulsion of milk.
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PMID:Decreased levels of connexin43 result in impaired development of the mammary gland in a mouse model of oculodentodigital dysplasia. 1845 14