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Journal articles on the topic 'Somatolactina'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Kakizawa, S., A. Ishimatsu, T. Takeda, T. Kaneko, and T. Hirano. "Possible involvement of somatolactin in the regulation of plasma bicarbonate for the compensation of acidosis in rainbow trout." Journal of Experimental Biology 200, no. 21 (1997): 2675–83. http://dx.doi.org/10.1242/jeb.200.21.2675.

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Somatolactin is a putative pituitary hormone of the growth hormone/prolactin family in fish. Its function is still unknown. The effects of environmental hypercapnia and hypoxia, acid (HCl) infusion and exhaustive exercise on plasma somatolactin levels were examined in the chronically cannulated rainbow trout to study the possible physiological roles of somatolactin. Respiratory acidosis induced by hypercapnia (2% CO2) did not affect plasma somatolactin level. In contrast, metabolic acidosis induced by acid infusion and exercise increased plasma somatolactin level. Blood pH was depressed to a s

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2

Kaneko, T., and T. Hirano. "ROLE OF PROLACTIN AND SOMATOLACTIN IN CALCIUM REGULATION IN FISH." Journal of Experimental Biology 184, no. 1 (1993): 31–45. http://dx.doi.org/10.1242/jeb.184.1.31.

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The endocrine control of calcium metabolism in fish is performed by hyper- and hypocalcaemic hormones as in terrestrial vertebrates. However, the hormones involved in calcium regulation in fish, which lack parathyroid glands, differ from those in terrestrial vertebrates. The pituitary is important in hypercalcaemic regulation in fish; prolactin exerts a hypercalcaemic action in addition to its well- established hypernatraemic effect. However, alternation of plasma calcium concentration may not be the primary factor influencing prolactin secretion; changes in osmolality or sodium levels seem to

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3

Azuma, Morio, Tsunehiro Suzuki, Hiroshi Mochida та ін. "Polymorphism of somatolactin-producing cells in the goldfish pituitary: immunohistochemical investigation for somatolactin-α and -β". Cell and Tissue Research 350, № 1 (2012): 167–76. http://dx.doi.org/10.1007/s00441-012-1435-3.

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4

FUKADA, HARUHISA. "Cloning of somatolactin receptor gene in Salmonidae." Newsletter of Japan Society for Comparative Endocrinology, no. 117 (2005): 15–18. http://dx.doi.org/10.5983/nl2001jsce.2005.117_15.

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5

May, Denise, Christopher M. Todd, and Mariann Rand-Weaver. "cDNA cloning of eel (Anguilla anguilla) somatolactin." Gene 188, no. 1 (1997): 63–67. http://dx.doi.org/10.1016/s0378-1119(96)00777-9.

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6

Zhu, Yong, Yasutoshi Yoshiura, Kiyoshi Kikuchi, Katsumi Aida, and Peter Thomas. "Cloning and Phylogenetic Relationship of Red Drum Somatolactin cDNA and Effects of Light on Pituitary Somatolactin mRNA Expression." General and Comparative Endocrinology 113, no. 1 (1999): 69–79. http://dx.doi.org/10.1006/gcen.1998.7180.

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7

Duguay, S. J., P. Swanson, and W. W. Dickhoff. "Differential expression and hormonal regulation of alternatively spliced IGF-I mRNA transcripts in salmon." Journal of Molecular Endocrinology 12, no. 1 (1994): 25–37. http://dx.doi.org/10.1677/jme.0.0120025.

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ABSTRACT Salmon have been shown to express alternatively spliced IGF-I mRNA transcripts coding for four different IGF-I prohormones. These transcripts, now designated Ea-1, Ea-2, Ea-3 and Ea-4, differ in size due to the inclusion of additional sequences in the E domain-coding region of the molecule. In this study, the tissue distribution and hormonal regulation of expression of alternatively spliced IGF-I mRNA transcripts were investigated in coho salmon. IGF-I mRNAs were detected by solution hybridization/RNase protection assay in all tissues examined. GH treatment significantly increased hep

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8

Zhu, Y., JW Stiller, MP Shaner, A. Baldini, JL Scemama, and AA Capehart. "Cloning of somatolactin alpha and beta cDNAs in zebrafish and phylogenetic analysis of two distinct somatolactin subtypes in fish." Journal of Endocrinology 182, no. 3 (2004): 509–18. http://dx.doi.org/10.1677/joe.0.1820509.

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Somatolactin (SL) is a pituitary hormone belonging to the growth hormone/prolactin superfamily, with recognizable homologues in all fish taxa examined to date. Although sequences from most fish share reasonably high sequence identity, several more highly divergent SLs have been reported. Goldfish SL and a second SL protein found in rainbow trout (rtSLP) are remarkably different from each other and also dissimilar to other SLs. It has been unclear whether rtSLP is a recent paralogue restricted to rainbow trout, or reflects a more ancient duplication of the SL gene, and whether it is related to

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9

Jiang, Quan, Mulan He, Xinyan Wang та Anderson O. L. Wong. "Grass carp somatolactin: II. Pharmacological study on postreceptor signaling mechanisms for PACAP-induced somatolactin-α and -β gene expression". American Journal of Physiology-Endocrinology and Metabolism 295, № 2 (2008): E477—E490. http://dx.doi.org/10.1152/ajpendo.90386.2008.

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Somatolactin (SL), the latest member of the growth hormone/prolactin family, is a novel pituitary hormone with diverse functions. However, the signal transduction mechanisms responsible for SL expression are still largely unknown. Using grass carp as an animal model, we examined the direct effects of pituitary adenylate cyclase-activating polypeptide (PACAP) on SL gene expression at the pituitary level. In primary cultures of grass carp pituitary cells, SLα and SLβ mRNA levels could be elevated by PACAP via activation of PAC-I receptors. With the use of a pharmacological approach, the AC/cAMP/

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10

Jiang, Quan, Wendy K. W. Ko, Ethan A. Lerner, K. M. Chan та Anderson O. L. Wong. "Grass carp somatolactin: I. Evidence for PACAP induction of somatolactin-α and -β gene expression via activation of pituitary PAC-I receptors". American Journal of Physiology-Endocrinology and Metabolism 295, № 2 (2008): E463—E476. http://dx.doi.org/10.1152/ajpendo.90385.2008.

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Somatolactin (SL), the latest member of the growth hormone/prolactin family, is a novel pituitary hormone with diverse functions. At present, SL can be identified only in fish but not in tetrapods and its regulation at the pituitary level has not been fully characterized. Using grass carp as a model, we examined the direct effects of pituitary adenylate cyclase-activating polypeptide (PACAP) on SL secretion and synthesis at the pituitary cell level. As a first step, the structural identity of grass carp SL, SLα and SLβ, was established by 5′/3′-rapid amplification of cDNA ends. These two SL is

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11

Jiang, Quan, та Anderson O. L. Wong. "Signal transduction mechanisms for autocrine/paracrine regulation of somatolactin-α secretion and synthesis in carp pituitary cells by somatolactin-α and -β". American Journal of Physiology-Endocrinology and Metabolism 304, № 2 (2013): E176—E186. http://dx.doi.org/10.1152/ajpendo.00455.2012.

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Pituitary hormones can act locally via autocrine/paracrine mechanisms to modulate pituitary functions, which represents an interesting aspect of pituitary regulation other than the traditional hypothalamic input and feedback signals from the periphery. Somatolactin, a member of the growth hormone (GH)/prolactin (PL) family, is a pleiotropic hormone with diverse functions, but its pituitary actions are still unknown. Recently, two SL isoforms, SLα and SLβ, have been cloned in grass carp. Based on the sequences obtained, recombinant proteins of carp SLα and SLβ with similar bioactivity in induci

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12

Hu, Qiongyao, Qinbo Qin, Shaohua Xu, et al. "Pituitary Actions of EGF on Gonadotropins, Growth Hormone, Prolactin and Somatolactins in Grass Carp." Biology 9, no. 9 (2020): 279. http://dx.doi.org/10.3390/biology9090279.

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In mammals, epidermal growth factor (EGF) plays a vital role in both pituitary physiology and pathology. However, the functional role of EGF in the regulation of pituitary hormones has rarely reported in teleost. In our study, using primary cultured grass carp pituitary cells as an in vitro model, we examined the effects of EGF on pituitary hormone secretion and gene expression as well as the post-receptor signaling mechanisms involved. Firstly, we found that EGF significantly reduced luteinizing hormone (LHβ) mRNA expression via ErbB1 coupled to ERK1/2 pathway, but had no effect on LH release

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13

Rand-Weaver, M., T. G. Pottinger, and J. P. Sumpter. "Plasma somatolactin concentrations in salmonid fish are elevated by stress." Journal of Endocrinology 138, no. 3 (1993): 509–15. http://dx.doi.org/10.1677/joe.0.1380509.

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ABSTRACT The preliminary finding that plasma levels of somatolactin (SL) were markedly elevated following stress caused by confinement in chinook salmon (Oncorhynchus tshawytscha) prompted a more detailed study of SL dynamics during stress. SL levels have been determined in the plasma of rainbow trout (Oncorhynchus mykiss) during exposure to acute (0–30 min) and short (0–24 h) periods of stress resulting from handling and confinement. The results show that SL levels increase rapidly within minutes following the onset of stress, reach a peak between 1 and 2 h, decline over the next 3 h, and the

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14

Rand-Weaver, M., T. G. Pottinger, and J. P. Sumpter. "Pronounced seasonal rhythms in plasma somatolactin levels in rainbow trout." Journal of Endocrinology 146, no. 1 (1995): 113–19. http://dx.doi.org/10.1677/joe.0.1460113.

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Abstract The aim of this study was to establish whether there are seasonal or age-related changes in circulating levels of somatolactin (SL) in rainbow trout (Onchorhynchus mykiss). SL levels were determined in blood sampled at monthly intervals over a 2-year period from a population of rainbow trout maintained under a natural daylength and temperature regime (North-West England, latitude 54°20′ N). SL levels displayed a distinct circannual cycle, with peak levels in summer (17–20 μg/l) and lowest levels occurring in winter (0·2–2 μg/l). This variation in SL levels was closely correlated with

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15

Lopez, Mauricio, Gabriela Nica, Patrick Motte, Joseph A. Martial, Matthias Hammerschmidt та Marc Muller. "Expression of the somatolactin β gene during zebrafish embryonic development". Gene Expression Patterns 6, № 2 (2006): 156–61. http://dx.doi.org/10.1016/j.modgep.2005.06.010.

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16

Ayson, Felix G., Evelyn Grace T. de Jesus, Yutaka Amemiya, Shunsuke Moriyama, Tetsuya Hirano, and Hiroshi Kawauchi. "Isolation and cDNA Cloning of Somatolactin in Rabbitfish (Siganus guttatus)." General and Comparative Endocrinology 115, no. 2 (1999): 292–300. http://dx.doi.org/10.1006/gcen.1999.7315.

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17

Azuma, M., K. Wada, J. Leprince, et al. "The Octadecaneuropeptide Stimulates Somatolactin Release from Cultured Goldfish Pituitary Cells." Journal of Neuroendocrinology 25, no. 3 (2013): 312–21. http://dx.doi.org/10.1111/jne.12005.

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18

Pendón, Carlos, Juan Pedro Martinez-Barberá, and Manuel M. Valdivia. "Cloning of a somatolactin-encoding cDNA from sole (Solea senegalensis)." Gene 147, no. 2 (1994): 227–30. http://dx.doi.org/10.1016/0378-1119(94)90071-x.

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19

Pendón, Carlos, J. Pedro Martı́nez-Barberá, Manuela Ortı́z, and Manuel M. Valdivia. "Bacterial Production and Purification of the Fish Pituitary Hormone Somatolactin." Protein Expression and Purification 7, no. 4 (1996): 389–94. http://dx.doi.org/10.1006/prep.1996.0058.

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20

Ocampo Daza, Daniel, and Dan Larhammar. "Evolution of the growth hormone, prolactin, prolactin 2 and somatolactin family." General and Comparative Endocrinology 264 (August 2018): 94–112. http://dx.doi.org/10.1016/j.ygcen.2018.01.007.

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21

Tanaka, Mio, Morio Azuma, Yumika Nejigaki, et al. "Melanin-concentrating hormone reduces somatolactin release from cultured goldfish pituitary cells." Journal of Endocrinology 203, no. 3 (2009): 389–98. http://dx.doi.org/10.1677/joe-09-0330.

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Melanin-concentrating hormone (MCH)-containing neurons directly innervate the adenohypophysis in the teleost pituitary. We examined immunohistochemically the relationship between MCH-containing nerve fibres or endings and somatolactin (SL)-producing cells in the goldfish pituitary. Nerve fibres or endings with MCH-like immunoreactivity were identified in the neurohypophysis in close proximity to the adenohypophysial cells showing SL-like immunoreactivity. We also examined the effect of MCH on SL release from cultured goldfish pituitary cells and SL synthesis using a cell immunoblot and a real-

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22

Company, Rubén, Josep Alvar Calduch-Giner, Mónica Mingarro, and Jaume Pérez-Sánchez. "cDNA cloning and sequence of European sea bass (Dicentrarchus labrax) somatolactin." Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 127, no. 2 (2000): 183–92. http://dx.doi.org/10.1016/s0305-0491(00)00250-9.

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23

Cánepa, Maximiliano Martín, Matías Pandolfi, María Cristina Maggese, and Paula Gabriela Vissio. "Involvement of somatolactin in background adaptation of the cichlid fishCichlasoma dimerus." Journal of Experimental Zoology Part A: Comparative Experimental Biology 305A, no. 5 (2006): 410–19. http://dx.doi.org/10.1002/jez.a.273.

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24

Planas, Josep V., Penny Swanson, Mariann Rand-Weaver, and Walton W. Dickhoff. "Somatolactin stimulates in vitro gonadal steroidogenesis in coho salmon, Oncorhynchus kisutch." General and Comparative Endocrinology 87, no. 1 (1992): 1–5. http://dx.doi.org/10.1016/0016-6480(92)90142-7.

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25

Sakai, M., M. Kobayashi, and H. Kawauchi. "In vitro activation of fish phagocytic cells by GH, prolactin and somatolactin." Journal of Endocrinology 151, no. 1 (1996): 113–18. http://dx.doi.org/10.1677/joe.0.1510113.

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Abstract The activation of rainbow trout (Oncorhynchus mykiss) phagocytic cells by chum salmon GH, prolactin (PRL) and somatolactin (SL) was investigated in vitro. Rainbow trout kidney leucocytes were cultured in RPMI 1640 medium containing 1, 10, 50 or 100 ng of each hormone/ml and the production of superoxide anion was measured using reduction of nitroblue tetrazolium (NBT) and ferricytochrome C. Macrophages incubated with 10–100 ng GH or PRL/ml showed significantly enhanced production of superoxide anion in both the NBT and ferricytochrome C tests compared with control macrophages (without

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26

Ono, M. "Pit-1/GH factor-1 involvement in the gene expression of somatolactin." Molecular Endocrinology 8, no. 1 (1994): 109–15. http://dx.doi.org/10.1210/me.8.1.109.

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27

Zhu, Yong, and Peter Thomas. "Effects of Light on Plasma Somatolactin Levels in Red Drum (Sciaenops ocellatus)." General and Comparative Endocrinology 111, no. 1 (1998): 76–82. http://dx.doi.org/10.1006/gcen.1998.7092.

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28

Amemiya, Yutaka, Yuji Sogabe, Masumi Nozaki, Akiyoshi Takahashi, and Hiroshi Kawauchi. "Somatolactin in the White Sturgeon and African Lungfish and Its Evolutionary Significance." General and Comparative Endocrinology 114, no. 2 (1999): 181–90. http://dx.doi.org/10.1006/gcen.1998.7250.

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29

Leng, X. Q., C. J. Li, and H. Cao. "Expression pattern of somatolactin in the Chinese sturgeon, Acipenser sinensis Gray, 1835." Journal of Applied Ichthyology 30, no. 6 (2014): 1222–28. http://dx.doi.org/10.1111/jai.12587.

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30

Ono, M., T. Harigai, T. Kaneko, Y. Sato, S. Ihara, and H. Kawauchi. "Pit-1/GH factor-1 involvement in the gene expression of somatolactin." Molecular Endocrinology 8, no. 1 (1994): 109–15. http://dx.doi.org/10.1210/mend.8.1.8152425.

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31

Wan, Guohui, and King Ming Chan. "A study of somatolactin actions by ectopic expression in transgenic zebrafish larvae." Journal of Molecular Endocrinology 45, no. 5 (2010): 301–15. http://dx.doi.org/10.1677/jme-09-0173.

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Somatolactin (SL) is a fish-specific hormone that belongs to the prolactin (PRL) and GH family. Recently, two forms of SL, SLα and SLβ, have been found in some species, and may have different actions and functions. To investigate the role of SL in fish growth and metabolism, we generated transgenic fish founders with ectopic expression of SLα and SLβ to study the physiological functions and actions of these SLs among several marker genes. We fused the cDNAs encoding the precursor SLs in frame to a zebrafish β-actin gene promoter to generate transgenic zebrafish lines that were coinjected with

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32

Rand-Weaver, Mariann, Bridget J. Baker, and Hiroshi Kawauchi. "Cellular localization of somatolactin in the pars intermedia of some teleost fishes." Cell and Tissue Research 263, no. 2 (1991): 207–15. http://dx.doi.org/10.1007/bf00318762.

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33

Fukamachi, Shoji, Takashi Yada, Axel Meyer, and Masato Kinoshita. "Effects of constitutive expression of somatolactin alpha on skin pigmentation in medaka." Gene 442, no. 1-2 (2009): 81–87. http://dx.doi.org/10.1016/j.gene.2009.04.010.

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34

Kakizawa, S., T. Kaneko, and T. Hirano. "Elevation of plasma somatolactin concentrations during acidosis in rainbow trout (Oncorhynchus mykiss)." Journal of Experimental Biology 199, no. 5 (1996): 1043–51. http://dx.doi.org/10.1242/jeb.199.5.1043.

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Somatolactin (SL) is a putative pituitary hormone of the growth hormone (GH)/prolactin (PRL) family in fish; its physiological function has yet to be determined. Acidosis was induced in rainbow trout (Oncorhynchus mykiss) by exposure to acidic water (pH 4.5) or by exhaustive exercise, and plasma concentrations of SL, PRL and GH as well as other plasma parameters were examined. A decrease in blood pH was observed in fish from 1 day after water acidification until the end of the experiment at day 7. Plasma SL levels in the acid-exposed fish increased, reached a peak on day 1 and then returned to

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35

Azuma, Morio, Mio Tanaka, Yumika Nejigaki, et al. "Pituitary adenylate cyclase-activating polypeptide induces somatolactin release from cultured goldfish pituitary cells." Peptides 30, no. 7 (2009): 1260–66. http://dx.doi.org/10.1016/j.peptides.2009.03.011.

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36

Jiang, Quan, та Anderson O. L. Wong. "Somatostatin-28 inhibitory action on somatolactin-α and -β gene expression in goldfish". American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 307, № 6 (2014): R755—R768. http://dx.doi.org/10.1152/ajpregu.00193.2014.

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Somatostain (SS) is known to inhibit growth hormone (GH) and prolactin (PRL) secretion. Somatolactin (SL) is a member of the GH/PRL family, but its regulation by goldfish brain somatostatin-28 (gbSS-28) has not been examined. To this end, the structural identity of goldfish SLα was established by 5′/3′-rapid amplification of cDNA ends. As revealed by in situ hybridization and immunohistochemical staining, the expression of SL isoforms was detected in pituitary cells located in the neurointermediate lobe (NIL). The transcripts of goldfish SS receptor 5a (Sst5a) but not Sst1b, Sst2, or Sst3a wer

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37

Smal, J., M. Rand-Weaver, J. P. Sumpter, P. Martin, T. G. Pottinger, and A. Guest. "Somatolactin and Growth Hormone Are Differentially Correlated To Various Metabolic Parameters in Trout." Netherlands Journal of Zoology 45, no. 1-2 (1994): 129–31. http://dx.doi.org/10.1163/156854295x00744.

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38

Rand-Weaver, Mariann, and Penny Swanson. "Plasma somatolactin levels in coho salmon (Oncorhynchus kisutch) during smoltification and sexual maturation." Fish Physiology and Biochemistry 11, no. 1-6 (1993): 175–82. http://dx.doi.org/10.1007/bf00004564.

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39

Kakizawa, Sho, Toyoji Kaneko, Tsuyoshi Ogasawara, and Tetsuya Hirano. "Changes in plasma somatolactin levels during spawning migration of chum salmon (Oncorhynchus keta)." Fish Physiology and Biochemistry 14, no. 2 (1995): 93–101. http://dx.doi.org/10.1007/bf00002453.

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40

Cheng, Kwai-Wa, Yuk-Hang Chan, Ya-Di Chen, Kei-Li Yu, and King Ming Chan. "Sequence of a cDNA Clone Encoding a Novel Somatolactin in Goldfish,Carassius auratus." Biochemical and Biophysical Research Communications 232, no. 2 (1997): 282–87. http://dx.doi.org/10.1006/bbrc.1997.6271.

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41

Mousa, Mostafa A., and Shaaban A. Mousa. "Implication of somatolactin in the regulation of sexual maturation and spawning ofMugil cephalus." Journal of Experimental Zoology 287, no. 1 (2000): 62–73. http://dx.doi.org/10.1002/1097-010x(20000615)287:1<62::aid-jez8>3.0.co;2-0.

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42

Ocampo Daza, Daniel, Görel Sundström, Tomas A. Larsson, and Dan Larhammar. "Evolution of the Growth Hormone-Prolactin-Somatolactin System in Relation to Vertebrate Tetraploidizations." Annals of the New York Academy of Sciences 1163, no. 1 (2009): 491–93. http://dx.doi.org/10.1111/j.1749-6632.2008.03671.x.

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43

Ono, M., Y. Takayama, M. Rand-Weaver, et al. "cDNA cloning of somatolactin, a pituitary protein related to growth hormone and prolactin." Proceedings of the National Academy of Sciences 87, no. 11 (1990): 4330–34. http://dx.doi.org/10.1073/pnas.87.11.4330.

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44

Herrero-Turrión, Javier, Almudena Velasco, Raquel Rodríguez, José Aijón, and Juan Lara. "Co-expression of somatolactin mRNAs in the pituitary gland of gilthead sea bream." Anatomy and Embryology 205, no. 5-6 (2002): 407–16. http://dx.doi.org/10.1007/s00429-002-0251-z.

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45

Kaneko, Toyoji, Sho Kakizawa, Takashi Yada, and Tetsuya Hirano. "Gene expression and intracellular localization of somatolactin in the pituitary of rainbow trout." Cell & Tissue Research 272, no. 1 (1993): 11–16. http://dx.doi.org/10.1007/bf00323565.

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46

Fukamachi, Shoji, Takashi Yada, and Hiroshi Mitani. "Medaka Receptors for Somatolactin and Growth Hormone: Phylogenetic Paradox Among Fish Growth Hormone Receptors." Genetics 171, no. 4 (2005): 1875–83. http://dx.doi.org/10.1534/genetics.105.048819.

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47

Mousa, Mostafa, Noha Khalil, Amal Hashem, and Mohamed Kora. "Immunohistochemical study of gonadotropin-releasing hormone and somatolactin during induced spawning of Liza ramada." Egyptian Journal of Histology 40, no. 3 (2017): 303–14. http://dx.doi.org/10.21608/ejh.2017.4657.

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48

Company, R., A. Astola, C. Pendón, M. M. Valdivia, and J. Pérez-Sánchez. "Somatotropic regulation of fish growth and adiposity: growth hormone (GH) and somatolactin (SL) relationship." Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology 130, no. 4 (2001): 435–45. http://dx.doi.org/10.1016/s1532-0456(01)00269-1.

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49

INGLETON, P. M., D. M. POWER, A. V. M. CANARIO, T. J. MARTIN, and J. A. DANKS. "Parathyroid Hormone-Related Protein and Somatolactin in Sea Bream (Sparus aurata) Brain and Pituitary." Annals of the New York Academy of Sciences 839, no. 1 TRENDS IN COM (1998): 370–71. http://dx.doi.org/10.1111/j.1749-6632.1998.tb10800.x.

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50

Fukamachi, S., M. Sugimoto, H. Mitani, and A. Shima. "Somatolactin selectively regulates proliferation and morphogenesis of neural-crest derived pigment cells in medaka." Proceedings of the National Academy of Sciences 101, no. 29 (2004): 10661–66. http://dx.doi.org/10.1073/pnas.0401278101.

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