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Cimi Ilmiawati Division of Histology and Cell Biology, Department of Anatomy, Jichi Medical University School of Medicine, 3311-1 Yakushiji, Shimotsuke, Tochigi 329-0498, Japan

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Kotaro Horiguchi Division of Histology and Cell Biology, Department of Anatomy, Jichi Medical University School of Medicine, 3311-1 Yakushiji, Shimotsuke, Tochigi 329-0498, Japan

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Ken Fujiwara Division of Histology and Cell Biology, Department of Anatomy, Jichi Medical University School of Medicine, 3311-1 Yakushiji, Shimotsuke, Tochigi 329-0498, Japan

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Takashi Yashiro Division of Histology and Cell Biology, Department of Anatomy, Jichi Medical University School of Medicine, 3311-1 Yakushiji, Shimotsuke, Tochigi 329-0498, Japan

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. For MMP-9 knockdown, a siRNA sequence against rat MMP-9 (SI102004247; Qiagen), with a nontargeting siRNA (1027283; Qiagen) as control, was transfected into cells by using an INTERFERin transfection reagent (PolyPlus Transfections, Inc., New York, NY

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Takehiro Tsukada Division of Histology and Cell Biology, Department of Anatomy, Jichi Medical University School of Medicine, Tochigi, Japan

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Morio Azuma Division of Histology and Cell Biology, Department of Anatomy, Jichi Medical University School of Medicine, Tochigi, Japan

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Kotaro Horiguchi Laboratory of Anatomy and Cell Biology, Department of Health Sciences, Kyorin University, Tokyo, Japan

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Ken Fujiwara Division of Histology and Cell Biology, Department of Anatomy, Jichi Medical University School of Medicine, Tochigi, Japan

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Tom Kouki Division of Histology and Cell Biology, Department of Anatomy, Jichi Medical University School of Medicine, Tochigi, Japan

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Motoshi Kikuchi Laboratory of Natural History, Jichi Medical University School of Medicine, Tochigi, Japan

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Takashi Yashiro Division of Histology and Cell Biology, Department of Anatomy, Jichi Medical University School of Medicine, Tochigi, Japan

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pituitary gland. Our group has identified various collagen types (type I, III, IV, and VI collagens) in rat anterior pituitary gland ( Kaidzu et al. 2000 ). These collagens are distributed around endocrine cells and capillaries and support tissue

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J. D. POWELL-JACKSON
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JAMES MACGREGOR
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M.R.C. Blood Pressure Unit, Western Infirmary, Glasgow, G11 6NT

(Received 27 August 1975)

The rat has been widely used in the investigation of the physiology and pathology of the renin—angiotensin system. This paper describes an adaptation of the radioimmunoassay of angiotensin II in human plasma (Dusterdieck & McElwee, 1971) for use in the rat.

Antibodies against [Asn1, Val5]-angiotensin II (Hypertensin, Ciba) were raised in rabbits using a minor modification of the method described by Goodfriend, Fasman, Kemp & Levine (1966). The antiserum used cross-reacted 100% with [Asp1, He5]-angiotensin II (Schwartz-Mann), 2–8 heptapeptide (Ile4), and 3–8 hexapeptide (Ile3) fragments but only 0·6% with [Asp1,Ile5]-angiotensin I and 0·008% with rat renin substrate obtained from dialysed nephrectomized rat plasma.

Since the octapeptide native to the rat is thought to be in the Ile5 form (Powell-Jackson, Brown, Lever, Macgregor, Macadam, Titterington, Robertson & Waite, 1972), [Asp1, Ile5]-angiotensin II was iodinated with Na125I as described

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W. G. North
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F. T. LaRochelle Jr
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G. R. Hardy
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Radioimmunoassays are described for vasopressin-associated rat neurophysin (VP-RNP), oxytocin-associated rat neurophysin (OT-RNP) and a major metabolic derivative of oxytocin-associated rat neurophysin (OT-RNP′). The cross-reactions in the radioimmunoassay for VP-RNP with preparations of OT-RNP and OT-RNP′ were 4 and 2%. However, the very small values found for VP-RNP using this radioimmunoassay in concentrated extracts of neural lobes from rats homozygous for the condition of hypothalamic diabetes insipidus (DI) indicate that the sum of the cross-reactions of OT-RNP and OT-RNP′ in the assay is <0·02%. The radioimmunoassay for OT-RNP showed a 100% cross-reaction with OT-RNP′ and a 4% cross-reaction with VP-RNP, while cross-reactions in the radioimmunoassay for OT-RNP′ with OT-RNP and VP-RNP were 17 and 3%. All three radioimmunoassays had a range of measurement from 20 to 1280 pg protein (2–132 fmol). The radioimmunoassays for VP-RNP and OT-RNP were used to measure neurophysin levels in the neural lobes and serum of Long–Evans rats and rats homozygous and heterozygous for DI. Neurophysin values in neural lobes were compared with values for oxytocin and vasopressin obtained by radioimmunoassay. On a molar basis the storage levels of vasopressin in Long–Evans rats were similar to those of VP-RNP; oxytocin levels were similar to the levels of total OT-RNP (OT-RNP + OT-RNP′). The storage levels in oxytocinergic and vasopressinergic neurones were similar. Total OT-RNP and oxytocin levels were similar in homozygous DI rats, while vasopressin and VP-RNP in these animals were <0·013 and <0·1% of the oxytocin and OT-RNP levels respectively. Long–Evans rats given 2% NaC1 for 96 h had drastically reduced storage of all four neurohypophysial peptides, but there was no significant change in their subcellular distribution when compared with control animals. This is taken as evidence that the readily releasable pool is not extragranular. Oxytocin and total OT-RNP were reduced to about 50% by depriving homozygous DI rats of water for 24 h. The storage levels of oxytocin and OT-RNP in female homozygous DI rats were twice those of their male counterparts. Normal serum values of VP-RNP and OT-RNP were 221±41 and 312±43 ng/l for males, and 280 ± 40 and 462±116 ng/l for females. Heterozygous DI rats (all female) had serum values of 165 ± 5 ng VP-RNP/1 and 1130±136 ng OT-RNP/1. In the serum of homozygous DI rats VP-RNP levels were below detectable limits; OT-RNP levels of rats with free access to water were 442± 37 ng/l for males and 959 ± 121 ng/l for females. These values are approximately twice those in Long–Evans rats. In water-deprived homozygous DI rats values of OT-RNP were increased threefold to 1202± 87 ng/l in males and twofold to 1822± 259 ng/l in females. Data indicate that female DI rats have twice the production/release rate of OT-RNP as males.

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Helena C Barbosa
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Silvana Bordin Departamento de Fisiologia e Biofísica, Departamento de Fisiologia e Biofísica, Beta Cell Development and Function Group, CENEXA, Instituto de Biologia, Universidade Estadual de Campinas, 13083-970 Campinas-SP, São Paulo-SP, Brazil

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Gabriel Anhê Departamento de Fisiologia e Biofísica, Departamento de Fisiologia e Biofísica, Beta Cell Development and Function Group, CENEXA, Instituto de Biologia, Universidade Estadual de Campinas, 13083-970 Campinas-SP, São Paulo-SP, Brazil

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Shanta J Persaud Departamento de Fisiologia e Biofísica, Departamento de Fisiologia e Biofísica, Beta Cell Development and Function Group, CENEXA, Instituto de Biologia, Universidade Estadual de Campinas, 13083-970 Campinas-SP, São Paulo-SP, Brazil

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James Bowe Departamento de Fisiologia e Biofísica, Departamento de Fisiologia e Biofísica, Beta Cell Development and Function Group, CENEXA, Instituto de Biologia, Universidade Estadual de Campinas, 13083-970 Campinas-SP, São Paulo-SP, Brazil

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Maria I Borelli Departamento de Fisiologia e Biofísica, Departamento de Fisiologia e Biofísica, Beta Cell Development and Function Group, CENEXA, Instituto de Biologia, Universidade Estadual de Campinas, 13083-970 Campinas-SP, São Paulo-SP, Brazil

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Juan J Gagliardino Departamento de Fisiologia e Biofísica, Departamento de Fisiologia e Biofísica, Beta Cell Development and Function Group, CENEXA, Instituto de Biologia, Universidade Estadual de Campinas, 13083-970 Campinas-SP, São Paulo-SP, Brazil

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Antonio C Boschero
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to either normal adult mice and dogs or streptozotocin-induced diabetic mice induced an increase in β-cell mass and signs of neogenesis ( Rosenberg et al . 2004 , Pittenger et al . 2007 ). In addition, neonatal and adult normal rat islets cultured

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Carmen Sanz Department of Biochemistry and Molecular Biology, Faculty of Medicine, Complutense University, 28040 Madrid, Spain

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Isabel Roncero Department of Biochemistry and Molecular Biology, Faculty of Medicine, Complutense University, 28040 Madrid, Spain

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Patricia Vázquez Department of Biochemistry and Molecular Biology, Faculty of Medicine, Complutense University, 28040 Madrid, Spain

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M Angeles Navas Department of Biochemistry and Molecular Biology, Faculty of Medicine, Complutense University, 28040 Madrid, Spain

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Enrique Blázquez Department of Biochemistry and Molecular Biology, Faculty of Medicine, Complutense University, 28040 Madrid, Spain

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activity in GT1-7 and rat hypothalamic slices. Materials and Methods Experimental animals All procedures involving animals were approved by the appropriate institutional review committee and met the guidelines

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V. W. K. Lee
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N. C. Kraft
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R. C. Atkins
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H. G. Burger
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ABSTRACT

Ovaries from rats treated with pregnant mare serum gonadotrophin were used as a source of inhibin for raising monoclonal antibodies. The antisera were screened for binding to rat ovarian tissue sections and examined for their ability to neutralize inhibin bioactivity in vitro, i.e. the ability to abolish the suppressive action of rat inhibin on pituitary FSH secretion. Two monoclonal antibodies to rat ovarian inhibin were raised, one exhibiting complete (antibody PHM15) and the other incomplete (antibody MCA-3) neutralizing ability. Both antisera bound well to antral granulosa cells, as judged by the degree of staining using an indirect horseradish peroxidase technique. Ascites fluid from mice injected with hybridoma cells secreting antibody PHM15 also showed inhibin-neutralizing ability, and was effective against inhibin prepared from ovarian follicular fluid of rats, sheep, pigs and cows. The latter observation indicates the potential application of this antibody to the preparation and measurement of inhibin from several animal species.

J. Endocr. (1986) 109, 379–383

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L. W. EDDIE
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H. W. G. BAKER
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A. DULMANIS
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R. E. HIGGINSON
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B. HUDSON
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SUMMARY

Medium from cultures of mature rat seminiferous tubules contained a substance which suppressed, in a dose-related manner, the luteinizing hormone releasing hormone (LH-RH)-stimulated secretion of FSH by cultured rat pituitary cells. The secretion of LH was suppressed to a lesser extent and the basal secretion of both LH and FSH was inconsistently affected. Gel filtration on Sephadex G-100 did not fractionate the activity. The active material did not inhibit the secretion of TSH or destroy LH-RH and the activity was not due to testosterone or oestradiol in the medium. Control media from liver cultures were inactive. It is concluded that inhibin is present in media from cultures of rat seminiferous tubules.

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P. M. INGLETON
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D. M. ENSOR
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M. P. HANCOCK
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The development of trophic hormones in foetal pituitary cells has been shown by the use of fluorescent antibodies, differential staining techniques and bioassay of pituitary homogenates. In foetal rat pituitaries, growth hormone, thyrotrophin and adrenocorticotrophin have been detected by radioimmunoassay and bioassay (Contopoulos & Simpson, 1957; Phillips & Schmidt, 1958; Milkovic & Milkovic, 1962; Birge, Peake, Mariz & Daughaday, 1967); but prolactin has not been detected by these techniques.

During experiments involving disc electrophoresis of rat pituitary homogenates the pituitaries from foetal rats were examined and a protein band appeared in the gel in a position almost identical with that of prolactin in the maternal pituitary (Plate). Rat pituitary hormones separated by disc electrophoresis according to the method of Davis (1964) have been identified by Jones, Fisher, Lewis & Vanderlaan (1965). Prolactin is the hormone that has the greatest mobility in this system; maternal prolactin had an R F value

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Simona Romano Department of Biological and Environmental Sciences and Technologies, Ecotekne, Via Prov.le per Monteroni, 73100 Lecce, Italy

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Antonella Muscella Department of Biological and Environmental Sciences and Technologies, Ecotekne, Via Prov.le per Monteroni, 73100 Lecce, Italy

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Carlo Storelli Department of Biological and Environmental Sciences and Technologies, Ecotekne, Via Prov.le per Monteroni, 73100 Lecce, Italy

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Santo Marsigliante Department of Biological and Environmental Sciences and Technologies, Ecotekne, Via Prov.le per Monteroni, 73100 Lecce, Italy

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1, is expressed by rat thyroid ( Montiel & Jimenez 1998 ) and a relationship between thyroid function and several components of the renin-angiotensin system has been established ( Montiel et al. 1984 , Ruiz et al. 1987 , Catanzaro 1995

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