CHARACTERISTICS OF SALIVARY Α-Amylase OF THE MOUSE

Amerongen, A. van Nieuw; Oderkerk, C.H.; Vreugdenhil, Angie; Roukema, P.A.

doi:10.1016/b978-0-08-027349-5.50032-x

Cited by 5 publications

(13 citation statements)

References 8 publications

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confidence: 99%

Metabolism of Sialic Acids from Exogeneously Administered Sialyllactose and Mucin in Mouse and Rat

Nöhle¹,

Schauer²

1984

Hoppe-Seyler´s Zeitschrift für physiologische Chemie

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A mixture of-/V-acetyl- [4,5,6,7,8,[9][10][11][12][13][14] C]neuraminosyl-a(2-3(6))-galactosyl-0( 1 -4)-glucose ([ l4 C]sialyl-lactose) and TV-acetylneuraminosyl-a(2-3(6))-galactosyl-|3(l-4)-glucit-l-[ 3 H]ol (sialyl-[ 3 H)lactitol) as well as porcine submandibular gland mucin labeled with TV-acetyland yV-glycoloyl-[9-3 H]neuraminic acid were administered orally to mice. The distribution of the different isotopes was followed in blood, tissues and excretion products of the animals. One half of the [ 14 C]sialyl-lactose/sialyl-[ 3 H]lactitol mixture given orally was excreted unchanged in the urine. The other half was hydrolysed by sialidase and partly metabolized further, followed by the excretion of 30% of the 14 C-radioactivity as free 5,6,7,8,[9][10][11][12][13][14] C]neuraminic acid and 60% of this radioactivity in the form of nonanionic compounds including expired 14 C0 2 within 24 h. The l4 C-radioactivity derived from the [ 14 C]sialyl-lactose/sialyl-[ 3 H]lactitol mixture which remained in the bodies of fasted mice after 24 h was less than 1 %. In the case of well-fed mice, a higher amount of the sialic acid residues was metabolized. The bulk of radioactivity of the mucin was resorbed within 24 h. About 40% of the radioactivity administered was excreted by the urine within 48 h; 30% of this radioactivity represented sialic acid and 70% other anionic and non-anionic metabolic products. 60% of the radioactivity administered remained in the body, and bound 3 H-labeled sialic acids were isolated from liver. Enzymes:jV-Acetylneuraminate lyase, yV-acetylneuraminate pyruvate-lyase (EC 4.1.3.3); Sialidase, acylneuraminyl hydrolase (EC 3.2.1.18). A bbreviations: NeuSAc = yV-Acetyl-D-neuraminic acid; Neu5,9Ac 2 = JV-acetyl-9-0-acetyl-D-neuraminic acid; NeuSGc = yV-glycoloyl-D-neuraminic acid; NeuSAcyl = '-acyl-D-neuraminic acid; NeuSAc-lyase = W-acetylneuraminate lyase; ManNAc = W-acetyl-D-mannosamine; Sialyllactose = Neu5Aca(2-3(6))Gal0(l-4)Glc (mixture of (2-3)-and (2-6)-glycosidically bound NeuSAcJ; sialyllactitol = Neu5Aca(2-3(6))Gal/3(l-4)glucit-l-ol; [ l4 5,6,7,8,[9][10][11][12][13][14] C]Neu5Aca(2-3(6))Gal0(l-4)Glc;( 3 HJsialyl-lactose = [9-3 H]Neu5Aca(2-3(6))Gal/3(l-4)Glc; sialyl-l 3 H]lactitol = Neu5Aa*(2-3(6))Gal0(l-4)glucit-l-| 3 H]ol; [ 14 C]sialyl-lactitol = [4 5,6,7,8,9-14 C]Neu5Aca(2-3(6))Gal0(l-4)glucit-l-ol; [ 3 H]sialyl-lactitol= (9-3 HJNeu5Aca(2-3(6))Gal0(l-4)glucit-l-ol. Copyright © by Walter de Gruyter & Co -Berlin · New York Brought to you by | University of Queensland -UQ Library Authenticated Download Date | 6/24/15 12:27 AM 1458 U. Nöhle and R. Schauer Bd. 365 (l984)Sialyl-a(2-3)-[ 3 H]lactitol was injected intravenous-resorbed. This is followed either by excretion as ly into rats; the substance was rapidly excreted in the urine without decomposition.These studies show that part of the sialic acids bound to oligosaccharides and glycoproteins can be hydrolysed in intestine by sialidase and be free sialic acid or by metabolization at variable degrees, which apparently depends on the compound ...

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Metabolism of Sialic Acids from Exogeneously Administered Sialyllactose and Mucin in Mouse and Rat

Nöhle¹,

Schauer²

1984

Hoppe-Seyler´s Zeitschrift für physiologische Chemie

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“…In addition, sublingual and most minor mucous glands of humans and rats receive predominantly parasympathetic innervation and little, if any, adrenergic innervation (Templeton and Thulin, 1978;Rossoni et al, 1979). Consistent with this pattern of innervation, both exocrine mucin secretion (Culp et al, 1991) and sustained fluid secretion (Melvin et al, 1991) by sublingual glands are induced primarily by the muscarinic cholinergic pathway but are unresponsive to 3-adrenergic or cx1-adrenergic agonists (Putney et al, 1978;Nieuw Amerongen et al, 1980;Compton et al, 1981;Culp et al, 1991). In contrast, exocrine secretion by serous parotid glands and seromucous submandibular glands is induced primarily by the 1-adrenergic pathway, whereas fluid secretion is regulated mostly by muscarinic cholinergic and cl-adrenergic activation.…”

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confidence: 66%

Regulation of Mucous Acinar Exocrine Secretion with Age

Culp

Richardson

1996

J Dent Res

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Denny and co-workers (Navazesh et al., 1992) recently reported decreased concentrations of MG1 and MG2 mucins in resting and stimulated whole human saliva with age. The current study was therefore conducted to examine whether there is a corresponding attenuation with age in stimulus secretion coupling regulating mucous cell exocrine secretion. We utilized an in vitro model system, isolated rat sublingual acini, to evaluate the regulation of mucous cell exocrine secretion. Rat sublingual glands are similar to human sublingual and minor mucous glands, both histologically and in terms of their pattern of innervation, which is predominantly parasympathetic. Mucin secretion is thus activated primarily by muscarinic cholinergic agonist and to a lesser extent by vasoactive intestinal peptide (VIP), which is co-localized with acetylcholine in parasympathetic nerve terminals. We isolated sublingual mucous acini from five-month-old and 24-month-old rats and compared the concentration responses for mucin secretion induced by VIP and the muscarinic agonist, arecaidine propargyl ester (APE). Concentration-response curves for VIP were nearly identical for mucous acini from the five-month-old and 24-month-old animals. Values for basal secretion, maximal secretion, and EC50 (approximately equal to 200 nmol/L VIP) were statistically equivalent between both age groups. Concentration-response curves for APE were also very similar between age groups, with no statistically significant difference in basal secretion or EC50 values (approximately equal to 50 nmol/L APE). Maximal secretion was slightly less but statistically different for 24-month-old vs. five-month-old animals, 158% vs. 169% above basal secretion, respectively. Collectively, we found no substantial age-related changes in the secretory responsiveness of salivary mucous cells.

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“…Many biochemical and histochemical studies have appeared on salivary and pancreatic amylase [1,11]. The amylase complex on mouse chromosome 3 encodes both salivary and pancreatic amylase [9].…”

Section: Discussionmentioning

confidence: 99%

“…This result suggested that the origin of serum amylase in rat was the parotid gland . Amerongen et al [1] showed that the parotid amylase of mouse was partially identical to serum amylase by immunochemical studies . Arglebe, Bremer and Chilla [2] reported that activities of two salivary isoamylases in rat serum were increased by daily intraperitoneal injection of isoprenaline.…”

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Electrophoretic Behavior of Amylase in Mouse: The Parotid Gland is Major Source of Serum Amylase

Ikeno¹,

Matsushima²,

Ikeno³

1988

Experimental Animals

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Amylase activity in the saliva, salivary glands, serum, liver (perfused and non perfused) and pancreas was assayed and isoamylases were separated by electrophoresis in these organs using C57BR/cdJ and M . m, molossinus (Kor) mice. Amylase isozymes in the saliva, parotid gland, serum and liver were identical in both strains , respectively. Amylase activity in the liver was lower than that in the serum and liver amylase disappeared almost by perfusion.Major serum amylase was released from the parotid gland in intact animals.In the mouse, a-amylase (EC 3.2.1.1.) is one of the major secretory enzymes of the salivary glands and of the pancreas. Many studies have appeared on salivary and pancreatic amylase [1, 11] using not only mouse but also rats and human.The parotid gland is an organ which has the highest amylase activity [7]. We previously reported that parasympathomimetic and sympathomimetic agents affected rat parotid gland in two ways : stimulation of amylase secretion into the saliva and acceleration of amylase release into the blood [6]. Though amylase activity in the serum of rat is lower than that in the parotid gland, a constant activity is detected in normal rat. Amylase isozyme in the human serum were detected in two types : parotid-and pancreas-type by electrophoresis [10].The increased activity of salivary isoamylase in human serum was seen with inflammatory disturbances of the salivary glands.In rat serum, the majority of isoamylase is parotid-type amylase [7]. Administration of pilocarpine increased the parotidtype amylase in rat serum significantly but this increase was abolished in parotidectomized rat [8]. This result suggested that the origin of serum amylase in rat was the parotid gland . Amerongen et al. [1] showed that the parotid amylase of mouse was partially identical to serum amylase by immunochemical studies . Arglebe, Bremer and Chilla [2] reported that activities of two salivary isoamylases in rat serum were increased by daily intraperitoneal injection of isoprenaline.These results indicated clearly that the source of serum amylase was the parotid gland after stimulation by drugs or inflammation.In this report we describe the electrophoretic behavior of amylase in mice (C57BR/ cdJ and MM m. molossinus (Kor)) which have different electrophoretic forms respectively and describe the source organ of serum amylase in intact mouse. Materials and MethodsMale and female C 57 BR/cdJ mice were obtained from Charles River Japan Inc., (Japan) and Mus Musculs molossinus (Kor)

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CHARACTERISTICS OF SALIVARY Α-Amylase OF THE MOUSE

Cited by 5 publications

References 8 publications

Metabolism of Sialic Acids from Exogeneously Administered Sialyllactose and Mucin in Mouse and Rat

Metabolism of Sialic Acids from Exogeneously Administered Sialyllactose and Mucin in Mouse and Rat

Regulation of Mucous Acinar Exocrine Secretion with Age

Electrophoretic Behavior of Amylase in Mouse: The Parotid Gland is Major Source of Serum Amylase

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