Amylase in the thyroid gland

Otsu, N; Oami, Hiroshi; Okawa, M.; Aotsuka, S; Yokohari, R

doi:10.1007/bf00495048

Cited by 10 publications

(2 citation statements)

References 11 publications

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“…The source of these cancers may be the lung, parotid [reviewed in 2], cervix uteri [30], stomach [31]. thyroid [32], or thymus [17]. The salivary type isozyme pattern is produced by these cancers.…”

Section: Discussionmentioning

confidence: 99%

An Amylase-Producing Serous Cystadenocarcinoma of the Ovary

Hodes

Sisk²,

Karn³

et al. 1985

Oncology

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A patient with an amylase-producing serous cystadenocarcinoma of the ovary had elevated serum and urine amylase levels and high levels of amylase in pleural and ascitic fluids. Serum and urine amylase levels reflected both surgical removal of tumor mass and response to chemotherapy. Tumor homogenates had pronounced amylase activity. Salivary type amylase isozyme patterns were found in electrophoresis of samples from all sources. Ascites tumor cells were successfully cultured and salivary type amylase was found in the culture media throughout 5 passages. The tumor was classified by light microscopy as poorly differentiated serous cystadenocarcinoma. Ultrastructural studies on the tumor were consistent with that diagnosis. Amylase was detected in the cells of the tumor examined by the immunoperoxidase technique.

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Section: Discussionmentioning

confidence: 99%

An Amylase-Producing Serous Cystadenocarcinoma of the Ovary

Hodes

Sisk²,

Karn³

et al. 1985

Oncology

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“…α-Amylase is abundantly expressed in the pancreas and salivary glands, and has been detected in liver [26], thyroid [27], parotid gland [28], white blood cells [29], lung carcinoma tissues [30], and brain [3] in humans. There are five isoforms of α-amylase including three salivary α-amylases (isoforms AMY1A, AMY1B, and AMY1C) and two pancreatic α-amylases (isoforms AMY2A and AMY 2B) [31].…”

Section: Expression Of Endogenous α-Amylase In the Human Duodenummentioning

confidence: 99%

Regulatory Functions of α-Amylase in the Small Intestine Other than Starch Digestion: α-Glucosidase Activity, Glucose Absorption, Cell Proliferation, and Differentiation

Date¹

2021

New Insights Into Metabolic Syndrome

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Pancreatic α-amylase binds to the N-glycan of glycoproteins. Here, I will show that pancreatic α-amylase has regulatory functions in the small intestine other than starch digestion. These new functions were revealed by identification of α-amylase-binding proteins in the intestinal brush border membrane (BBM). This topic will include the following four parts: 1) identification of glycoproteins that bind pancreatic α-amylase in the small intestinal BBM; 2) interactions between pancreatic α-amylase and the binding glycoproteins, sucrose-isomaltase (α-glucosidase), and sodium/glucose co-transporter 1 (SGLT1), in which pancreatic α-amylase enhanced maltose degradation of sucrose-isomaltase under conditions including calcium and sodium, and inhibited glucose uptake of SGLT1; 3) localization of pancreatic α-amylase in the small intestine by binding to the BBM and being internalized into lysosomes through the endocytic pathway; and 4) expression of endogenous α-amylase in the duodenum: AMY2B, a pancreatic type α-amylase, is highly expressed in the human duodenum next to the pancreas. The α-amylase expression in the duodenum is required for proliferation and differentiation of human small intestinal epithelial cells.

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Immunohistochemical demonstration of pancreatic α-amylase and trypsin in intrahepatic bile ducts and peribiliary glands

Terada

Nakanuma

1991

Hepatology

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Epithelia of intrahepatic bile ducts and peribiliary glands were immunohistochemically examined for pancreatic alpha-amylase and trypsin in 54 normal autopsied livers. alpha-Amylase was evaluated with a polyclonal antibody, and trypsin was assayed with both polyclonal and monoclonal antibodies. alpha-Amylase was observed in large ducts, septal ducts and peribiliary glands in most livers and was seen in interlobular ducts in seven (13%) livers. Trypsin immunoreactivity with the polyclonal antibody was observed in peribiliary glands in 21 (39%) livers; it was absent in intrahepatic bile ducts in all but one liver. Trypsin immunoreactivity with the monoclonal antibody was present in large ducts, septal ducts and peribiliary glands in about 70% of the livers and was seen in interlobular ducts in two (4%) livers. Bile ductules were always negative for the two antigens. Some epithelia of peribiliary glands positive for both alpha-amylase and trypsin histologically resembled pancreatic acinar cells. alpha-Amylase and trypsin immunoreactivities of intrahepatic biliary epithelia and pancreatic aninar cells were eliminated by absorption of primary antibodies by alpha-amylase or trypsin, suggesting the specificities of the immunoreactivities. These data suggest that epithelia of intrahepatic large ducts, septal ducts and peribiliary glands contain pancreatic alpha-amylase in most livers and that they contain trypsin in about 70% of livers. alpha-Amylase and trypsin may be secreted into intrahepatic bile duct lumens, thereby exerting important effects on the physiology of the intrahepatic biliary tree and hepatic bile.

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Amylase in the thyroid gland

Cited by 10 publications

References 11 publications

An Amylase-Producing Serous Cystadenocarcinoma of the Ovary

An Amylase-Producing Serous Cystadenocarcinoma of the Ovary

Regulatory Functions of α-Amylase in the Small Intestine Other than Starch Digestion: α-Glucosidase Activity, Glucose Absorption, Cell Proliferation, and Differentiation

Immunohistochemical demonstration of pancreatic α-amylase and trypsin in intrahepatic bile ducts and peribiliary glands

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