An in Vitro Study of Pancreatic Ductal Cells

Singh, Manjit; Parks, N. M.; Webster, Peter

doi:10.3181/00379727-157-39982

Cited by 7 publications

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“…Singh et al (20) showed a decrease in the enzyme activity in ductal tissue with fasting. The results were significant (p <0.005) for activity per milligram protein and (p <0.05) for activity per milligram DNA.…”

Section: Discussionmentioning

confidence: 99%

“…Since a method has been recently developed for the use of bovine pancreatic ductal expiants in chemical carcinogenesis as well as in physiological studies (9,10), we have measured selected plasma membrane enzymes in the bovine main pancreatic duct and com-ate-dependent adenosine triphosphatase, EC 3.6.1.3), 5'-nucleotidase (EC 3.1.3.5), alkaline phosphatase (EC ' 3.1.3.1), and carbonate dehy dratase (EC 4.2.1.1). The first three enzymes have been previously measured in cat (24) and rat (6,20) pancreatic ductal and acinar prepara tions by other investigators. However, studies on bovine pancreas on these three enzymes have not been reported.…”

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Enzymic Profiles of Bovine Pancreatic Ductal and Acinar Tissues

Lakshmanan¹,

Kahng²,

Jones³

1979

Enzyme

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The plasma membrane enzymes, alkaline phosphatase, bicarbonate-dependent adenosine triphosphatase, 5'-nucleotidase, and carbonate dehydratase, were measured in ductal and acinar preparations of bovine pancreas. Epithelial cells were scraped from the main duct and a piece of acinar tissue was dissected from the whole pancreas for homogenization. All enzymes studied demonstrated higher levels in the duct per milligram protein than in the acinus: bicarbonate-dependent adenosine triphosphatase was 2.8 times higher; 5'-nucleotidase, 4.1 times higher; carbonate dehydratase, 16.9 times higher, while alkaline phosphatase showed only a slight increase in the duct compared to acini.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Enzymic Profiles of Bovine Pancreatic Ductal and Acinar Tissues

Lakshmanan¹,

Kahng²,

Jones³

1979

Enzyme

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“…Ducts have previously been obtained by micro-dissection from the pancreas of the cat (Wizemann, Christian, Wiechmann & Schulz, 1974), rat (Singh, Parks & Webster, 1978) and cow (Lakshmanan, Kohng & Jones, 1979). However, in only one of these studies (Wizemann et al 1974) were ducts smaller than either the main pancreatic or common bile/pancreatic duct obtained.…”

Section: Discussionmentioning

confidence: 99%

Isolation of Ducts From the Pancreas of Copper‐deficient Rats

et al. 1986

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SUMMARYA technique is described, involving tissue dissociation and micro-dissection, for the isolation of interlobular ducts from the pancreas of copper-deficient rats. The average length and outside diameter of the isolated ducts were 589 0+ 18 6 and 78 1 + 1 6 ,um (mean +S.E.M., n = 425) respectively. Between twenty and fifty ducts could be obtained from each pancreas. Frequently, the smaller intralobular ducts, which had outside diameters of between 15 and 25 ,um, were observed as branches of the interlobular ducts. Light and electron microscopy showed that the isolated ducts were structurally intact, and that the epithelial cells possessed all the typical ultrastructural features of duct cells within the gland of copper-replete rats. The isolated ducts consumed oxygen at a rate of 2 27 + 0 55 ml 02/min. 100 g wet weight duct epithelium (n = 6). The concentrations of ATP, ADP and AMP in the ducts were 3-78+0 81, 0 68+0-19 and 0-41 + 013 mmol/l duct epithelium (n = 8) respectively. These data give values for ATP: ADP and ATP:AMP ratios of 5 6:1 and 9-2:1 respectively, and an energy charge of 0 85+0 01 (n = 8) suggesting that the epithelial cells are healthy and in a stable metabolic state. In the presence of the phosphodiesterase inhibitor 3-isobutyl-l-methylxanthine (0-67 mM), the basal concentration ofcyclic AMP in the isolated ducts was 17 4 + 0-7 ,tmol/l duct epithelium (n = 3).Secretin (0 1 nM-1 /M) caused a dose-related increase in cyclic AMP content up to a maximum of 3760 + 85 3 ,umol/l duct epithelium (n = 4). This indicates that the epithelial cells possess secretin receptors, and that these receptors can be functionally linked to adenylate cyclase.

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“…The protein to DNA ratios of rat acinar cells (25) and the sieved filtrate (primarily acinar cells) are 31 and 37, whereas the ratios for isolated major rat pancreatic ducts (46) and the sieved filtrand (ducts and other nonacinar structures) are 8 .3 and 7 .4 . Thus, if the specific activity of a given enzyme were the same on a DNA basis, the acinar cell would have a fourfold lower specific activity of that enzyme when calculated on a protein basis.…”

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“…The isolation from collagenase digests of duct cells from the rat (42) and ductule fragments from the rat (15) and mouse (20) has been reported in abstract form . Pancreatic ducts have been obtained by dissection from the rat (46), cat (52), and cow (27) and have been analyzed for their content ofvarious enzymes. The ultrastructural characteristics of the isolated bovine ducts have been defined (22).…”

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Characterization of ducts isolated from the pancreas of the rat.

Githens¹,

Holmquist²,

Whelan³

et al. 1980

The Journal of Cell Biology

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Rat pancreases were minced and treated with collagenase or collagenase supplemented with chymotrypsin to yield a mixture of ducts, islets, acinar cell clusters, blood vessels, and nerves . Histologically and ultrastructurally, the isolated tissues resembled their in situ counterparts in most respects, the major difference being the destruction of the basement membranes (basal laminae) . Ducts ranging in size from the common bile/main pancreatic duct to the intercalated ducts were identified in the digest, although interlobular ducts were most frequently observed .Acinar tissue fragments were separated from nonacinar structures either by flotation through discontinuous gradients of Ficoll or by sieving, the latter technique being the more efficient . Common bile/main ducts, interlobular ducts, and blood vessels were selected manually from the nonacinar fractions . Biochemical analyses showed that the entire nonacinar fraction, as well as isolated ducts and blood vessels, contained larger alkaline phosphatase, carbonic anhydrase, and Mg-ATPase specific activities than acinar tissue, whereas acinar tissue contained larger y-glutamyltranspeptidase and amylase activities . However, >63% of the total recovered activity of each enzyme was associated with the acinar tissue . Both the association of the majority of each of these enzyme activities with the acinar tissue and the similarity in specific activities associated with ducts and blood vessels indicate that none of the enzymes tested is a unique marker for interlobular and larger ducts of the pancreas of the rat.Pancreatic ducts comprise a simple cuboidal to columnar epithelium (12,16,21) and a layer of connective tissue . The ducts serve as a conduit for the movement of exocrine enzymes from the acinar cells to the duodenum and they also produce at least part of the secretin-stimulated bicarbonaterich pancreatic fluid secretion (9, 44) . The role of the ducts in fluid/electrolyte secretion has been supported by ultrastructural (24) and micropuncture (29, 43) studies and by studies of the relatively unimpaired fluid/electrolyte secretion in rats whose acinar cells have been destroyed (14) .Carbonic anhydrase in the dog (4), (Na+K)-ATPase in the rabbit (40, 48), and HC03-ATPase in the dog and cat (45) have been implicated in pancreatic fluid secretion by experiments in which specific inhibitors (acetazolamide, ouabain, and thiocyanate, respectively) reduced fluid secretion by the intact pancreas . Histochemical studies have demonstrated the presence in the duct epithelium J. CELL BIOLOGY C The Rockefeller University Press

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An in Vitro Study of Pancreatic Ductal Cells

Cited by 7 publications

References 0 publications

Enzymic Profiles of Bovine Pancreatic Ductal and Acinar Tissues

Enzymic Profiles of Bovine Pancreatic Ductal and Acinar Tissues

Isolation of Ducts From the Pancreas of Copper‐deficient Rats

Characterization of ducts isolated from the pancreas of the rat.

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