BASAL AND STIMULATED PLASMA-LEVELS OF PANCREATIC AMYLIN INDICATE ITS CO-SECRETION WITH INSULIN IN HUMANS

被引:197
作者
HARTTER, E [1 ]
SVOBODA, T [1 ]
LUDVIK, B [1 ]
SCHULLER, M [1 ]
LELL, B [1 ]
KUENBURG, E [1 ]
BRUNNBAUER, M [1 ]
WOLOSZCZUK, W [1 ]
PRAGER, R [1 ]
机构
[1] LUDWIG BOLTZMANN INST KLIN ENDOKRINOL,VIENNA,AUSTRIA
关键词
AMYLIN; DIABETES ASSOCIATED POLYPEPTIDE; ISLET AMYLOID POLYPEPTIDE;
D O I
10.1007/BF00404025
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
Amylin is a 37-amino acid pancreatic polypeptide, probably involved in the pathophysiology of Type 2 (non-insulin-dependent) diabetes mellitus. We have determined amylin in human plasma by extraction-based radioimmunoassay (Sep-Pak C18). Of 23 healthy control subjects plasma amylin was determined as 11.9 +/- 3.5 ng/l. Of 27 patients with Type 2 diabetes receiving insulin the amylin levels were lower, and in 16 patients with Type 2 diabetes on oral medication they were higher than in the control subjects: 8.2 +/- 4.4 ng/l (p < 0.01) vs 18.8 +/- 9.9 ng/l (p < 0.05). In 14 Type 1 (insulin-dependent) diabetic patients we found extremely low mean amounts of amylin: 2.9 +/- 1.9 ng/l (p < 0.002). Thus, basal amylin appears to be associated with the capacity to release insulin. An oral glucose load stimulated the release of amylin, this was more pronounced in patients with Type 2 diabetes than in healthy subjects. An excellent correlation of mean amylin with mean insulin concentrations was obtained (r = 0.949). In patients with Type 2 diabetes amylin was reduced congruent to a decrease in C-peptide during a hyperinsulinaemic, euglycaemic glucose clamp experiment (r = 0.971 for linear correlation between C-peptide levels and amylin). We conclude, that amylin and insulin are co-secreted in humans, and that the amylin release is under feedback-control by insulin.
引用
收藏
页码:52 / 54
页数:3
相关论文
共 10 条
  • [1] EFFECTS OF MEAL INGESTION ON PLASMA AMYLIN CONCENTRATION IN NIDDM AND NONDIABETIC HUMANS
    BUTLER, PC
    CHOU, J
    CARTER, WB
    WANG, YN
    BU, BH
    CHANG, D
    CHANG, JK
    RIZZA, RA
    [J]. DIABETES, 1990, 39 (06) : 752 - 756
  • [2] COSECRETION OF AMYLIN AND INSULIN FROM ISOLATED RAT PANCREAS
    FEHMANN, HC
    WEBER, V
    GOKE, R
    GOKE, B
    ARNOLD, R
    [J]. FEBS LETTERS, 1990, 262 (02) : 279 - 281
  • [3] REDUCED ISLET-AMYLOID POLYPEPTIDE IN INSULIN-DEPENDENT DIABETES-MELLITUS
    HARTTER, E
    LELL, B
    LUDVIK, B
    SVOBODA, T
    SCHULLER, M
    WOLOSZCZUK, W
    PRAGER, R
    [J]. LANCET, 1990, 335 (8693) : 854 - 854
  • [4] JOHNSON KH, 1989, NEW ENGL J MED, V321, P513
  • [5] EVIDENCE OF COSECRETION OF ISLET AMYLOID POLYPEPTIDE AND INSULIN BY BETA-CELLS
    KAHN, SE
    DALESSIO, DA
    SCHWARTZ, MW
    FUJIMOTO, WY
    ENSINCK, JW
    TABORSKY, GJ
    PORTE, D
    [J]. DIABETES, 1990, 39 (05) : 634 - 638
  • [6] ISLET AMYLOID POLYPEPTIDE RESPONSE TO GLUCOSE, INSULIN, AND SOMATOSTATIN ANALOG ADMINISTRATION
    MITSUKAWA, T
    TAKEMURA, J
    ASAI, J
    NAKAZATO, M
    KANGAWA, K
    MATSUO, H
    MATSUKURA, S
    [J]. DIABETES, 1990, 39 (05) : 639 - 642
  • [7] ESTABLISHMENT OF RADIOIMMUNOASSAY FOR HUMAN ISLET AMYLOID POLYPEPTIDE AND ITS TISSUE CONTENT AND PLASMA-CONCENTRATION
    NAKAZATO, M
    ASAI, J
    KANGAWA, K
    MATSUKURA, S
    MATSUO, H
    [J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1989, 164 (01) : 394 - 399
  • [8] NISHI M, 1990, J BIOL CHEM, V265, P4173
  • [9] AMYLIN SECRETION FROM THE RAT PANCREAS AND ITS SELECTIVE LOSS AFTER STREPTOZOTOCIN TREATMENT
    OGAWA, A
    HARRIS, V
    MCCORKLE, SK
    UNGER, RH
    LUSKEY, KL
    [J]. JOURNAL OF CLINICAL INVESTIGATION, 1990, 85 (03) : 973 - 976
  • [10] ISLET-AMYLOID POLYPEPTIDE IN HUMAN-PLASMA
    VANJAARSVELD, BC
    HACKENG, WHL
    NIEUWENHUIS, MG
    ERKELENS, DW
    GEERDINK, RA
    LIPS, CJM
    [J]. LANCET, 1990, 335 (8680) : 60 - 60