A radioimmunoassay for mouse α-lactalbumin

Zamierowski, Marilyn M.; Ebner, Kurt E.

doi:10.1016/0022-1759(80)90126-x

Cited by 16 publications

(10 citation statements)

References 15 publications

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“…The RIA developed for mouse -lactalbumin I was specific and highly sensitive. Futhermore, the antiserum developed to -lactalbumin I was equally effective in recognizing both forms of the protein, which is in agreement with previous reports (Zamierowski & Ebner, 1980;Bhattacharjee & Vonderhaar, 1983). The placenta has been known for some time to play an important role in mammary gland development and differentiation during pregnancy in rodents (Nagasawa & Yanai, 1971;Knight & Peaker, 1982a,¿>;Bussmann, Koninckx & Deis, 1983).…”

Section: Discussionsupporting

confidence: 92%

“…The pi ranged from 5-35 to 5-10. Previous studies have reported the purification of (1) two charge isoforms of mouse -lactalbumin having the same molecular weight of approximately 14 500 (Zamierowski & Ebner, 1980; Bhattacharjee & Vonderhaar, 1983) and (2) a-lactalbumins with molecular weights of 14 100 and 18 500 (Nagamatsu & Oka, 1980). In the latter study the larger molecular weight form consisted of two charge isoforms, while the smaller molecular weight form consisted of four different charge isoforms.…”

Section: Discussionmentioning

confidence: 95%

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Lactogenic response of cultured mouse mammary epithelial cells to mouse placental lactogen

Thórdarson¹,

Villalobos²,

Colosi³

et al. 1986

Journal of Endocrinology

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The ability of mouse placental lactogen (mPL), mouse prolactin (mPRL), mouse GH (mGH) and ovine prolactin (oPRL) to stimulate synthesis of alpha-lactalbumin was tested in a primary culture of mouse mammary gland epithelial cells. Mammary tissue was obtained from 10-day pregnant Swiss Webster mice, enzymatically dissociated and the cells were cultured on floating collagen gels for 5 days. The basic culture medium consisted of Nutrient Mixture F12/Dulbecco's Modified Eagle's Medium (1:1, v/v), containing 10 mg insulin/1, 5 mg cortisol/l, 10 micrograms epidermal growth factor/l, 5 g bovine serum albumin/l and 50 mg gentamycin/l. Mouse PL, mPRL, mGH and oPRL were added to the basic medium in concentrations from 1 microgram/l to 1 mg/l. Accumulation of alpha-lactalbumin in the culture medium was measured. For that purpose, mouse alpha-lactalbumin was purified from mammary tissue obtained from lactating Swiss Webster mice and a radioimmunoassay was developed. Mouse PL, mPRL and oPRL stimulated a dose-dependent increase in alpha-lactalbumin secretion. Mouse GH also caused a significant, but dose-independent, increase in alpha-lactalbumin secretion. Mouse PL showed the greatest activity in stimulating alpha-lactalbumin secretion. It was concluded that mPL is an important lactogenic hormone in the latter half of pregnancy in the mouse, when circulating mPRL concentrations are low.

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Section: Discussionsupporting

confidence: 92%

Section: Discussionmentioning

confidence: 95%

Lactogenic response of cultured mouse mammary epithelial cells to mouse placental lactogen

Thórdarson¹,

Villalobos²,

Colosi³

et al. 1986

Journal of Endocrinology

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“…The cDNA corresponding to rat a-lacPalbumin has been cloned recently, showing that about 5 % of the mRNAs specific for the lactating rat mammary gland code for a-lactalbumin [15]. In the mouse milk, however, a-lactalbumin seems to be a much less abundant protein comprising not more than 0.85 of the total milk proteins [52]. We are in the process of screening further cDNA clones from the tissue-specific cDNA library in order to isolate cDNA clones coding for this minor mouse milk protein.…”

Section: Discussionmentioning

confidence: 99%

“…Based on an enzymatic assay, specific for a-lactalbumin, the 14.3-kDa protein had been assigned to a-lactalbumin [51]. Recently it was shown that a novel whey protein exists which is about twice as abundant as a-lactalbumin, which comigrates with a-lactalbumin on sodium dodecylsulfate/polyacrylamide gels [52] and which was named whey acidic protein [53]. By comparison with the whey proteins from other species the 67-kDa and 78-kDa protein could very well be milk serum albumin [21] and lactoferrin [50] of the mouse.…”

Section: Mouse and Rat Milk Proteinsmentioning

confidence: 99%

“…Applying ion-exchange chromatography as a further purification step of the 14.3-kDa milk protein, it had been shown recently that at least two proteins comigrate at this position on sodium dodecylsulfate/polyacrylamide gels. A minor one is a-lactalbumin [52] and a major one is an acidic whey protein [53], possibly identical to the 13.7-kDa protein product processed in vitro.…”

Section: Translation Of' Mouse and Rut Mummary Gland M R N A In Vitromentioning

confidence: 99%

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Characterization and Cloning of the mRNAs Specific for the Lactating Mouse Mammary Gland

Hennighausen

Sippel

1982

European Journal of Biochemistry

129

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We have characterized and cloned the lactation-specific mRNAs of mouse mammary glands. The group of eight milk-protein-specific mRNAs were identified (a) by size and antigenic properties of their translation products in vitro and (b) by characterization of their respective cDNA clones. Two x-caseins (43 kDa and 39 kDa) are encoded by mRNAs of 1600 nucleotides and two a-caseins (26 kDa) are encoded by mRNAs of 1450 nucleotides in length. Three smaller caseins, y-casein (23.7 kDa), &casein (21 kDa) and &-casein (14.5 kDa) are synthesized by mRNAs of 880, 1150 and 860 nucleotides. Beside these casein mRNAs a mammary specific 620 nucleotide mRNA codes for a novel acidic whey protein (13.7 kDa).cDNA clones corresponding to the mRNAs for the lactation-specific proteins have been isolated from a mammary-specific cDNA library. Cloned a-casein cDNA hybridizes to both cc-casein specific mRNAs and cloned a-casein cDNAs hybridize with both a-casein specific mRNAs. By RNA blot analysis we show that the cloned cDNAs for mouse a-casein, [)-casein, y-casein and &-casein and the acidic whey protein cross-hybridize with mRNAs of the rat, demonstrating partial sequence homology between the corresponding mRNAs of those species.

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The Mammary Gland

Vonderhaar

Bhattacharjee

1985

Biological Responses in Cancer

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A radioimmunoassay for mouse α-lactalbumin

Cited by 16 publications

References 15 publications

Lactogenic response of cultured mouse mammary epithelial cells to mouse placental lactogen

Lactogenic response of cultured mouse mammary epithelial cells to mouse placental lactogen

Characterization and Cloning of the mRNAs Specific for the Lactating Mouse Mammary Gland

The Mammary Gland

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