Decreased senescence marker protein-30 could be a factor that contributes to the worsening of glucose tolerance in normal aging

Hasegawa, Goji

doi:10.4161/isl.2.4.12157

Cited by 10 publications

(8 citation statements)

References 17 publications

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“…Choi et al reported similar findings [12]. The reason could be the age-related deterioration in the functioning of beta cells of the pancreas or the development of insulin resistance which appears later in life [12,28].…”

Section: Figure 1 Frequency Distribution Of Normal Glucose Tolerancesupporting

confidence: 65%

Frequency of impaired glucose tolerance and diabetes mellitus in subjects with fasting blood glucose below 6.1 mmol/L [110 mg/dL]

Khan¹,

Ijaz²,

Bokhari³

et al. 2013

East Mediterr Health J

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The diagnosis of diabetes mellitus by the available criteria is controversial and relies heavily on fasting glucose results. This cross-sectional study in 2010-2011 aimed to measure the frequency of impaired glucose tolerance and diabetes mellitus in 127 subjects having fasting blood glucose < 7.0 mmol/L and to measure the agreement between different standard diagnostic criteria. Subjects presenting to a laboratory for analysis of fasting blood glucose for excluding diabetes mellitus underwent a 2-hour 75 g oral glucose challenge. A total of 40.6% of subjects with fasting blood glucose from 5.6-6.0 mmol/L had abnormal glucose regulation on the basis of the gold standard glucose challenge. Agreement between American Diabetes Association and World Health Organization diagnostic criteria was only fair (kappa = 0.32). Abnormalities of glucose metabolism including impaired glucose tolerance and diabetes mellitus can exist at fasting blood glucose results < 6.1 mmol/L (110 mg/dL).

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Section: Figure 1 Frequency Distribution Of Normal Glucose Tolerancesupporting

confidence: 65%

Frequency of impaired glucose tolerance and diabetes mellitus in subjects with fasting blood glucose below 6.1 mmol/L [110 mg/dL]

Khan¹,

Ijaz²,

Bokhari³

et al. 2013

East Mediterr Health J

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“…For preventing a vitamin C deficiency, SMP30 knockout mice were supplemented with a sufficient amount of vitamin C. With the standard diet, SMP30 knockout mice at the age of 15 weeks showed mild glucose intolerance and impairment in acute insulin secretion after glucose administration compared with wild-type mice, yet they maintained still better peripheral insulin sensitivity as assessed by an insulin tolerance test. 35,36 Furthermore, feeding with a high-fat diet for 8 weeks severely exacerbated glucose tolerance in SMP30 knockout mice compared with that of wildtype mice, but there was no difference of the insulin sensitivity between SMP30 knockout and wild-type mice. The SMP30 deficiency did not affect pancreas weight, pancreatic insulin content or β-cell mass and proliferation in mice fed either the standard diet or high-fat diet.…”

Section: Smp30 and Glucose Intolerancementioning

confidence: 99%

“…To show the possible association of a reduction in SMP30 expression with the glucose metabolism disorder that occurs in older adults, we examined the role of SMP30 in glucose homeostasis by using SMP30 knockout mice. For preventing a vitamin C deficiency, SMP30 knockout mice were supplemented with a sufficient amount of vitamin C. With the standard diet, SMP30 knockout mice at the age of 15 weeks showed mild glucose intolerance and impairment in acute insulin secretion after glucose administration compared with wild‐type mice, yet they maintained still better peripheral insulin sensitivity as assessed by an insulin tolerance test . Furthermore, feeding with a high‐fat diet for 8 weeks severely exacerbated glucose tolerance in SMP30 knockout mice compared with that of wild‐type mice, but there was no difference of the insulin sensitivity between SMP30 knockout and wild‐type mice.…”

Section: Smp30 and Glucose Intolerancementioning

confidence: 99%

Involvement of senescence marker protein‐30 in glucose metabolism disorder and non‐alcoholic fatty liver disease

Kondo

Ishigami

2016

Geriatrics Gerontology Int

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Senescence marker protein-30 (SMP30) was found to decrease in the liver, kidneys and lungs of mice during aging. SMP30 is a pleiotropic protein that acts to protect cells from apoptosis by enhancing plasma membrane Ca 2+ -pump activity and is bona fide gluconolactonase (EC 3.1.1.17) that participates in the penultimate step of the vitamin C biosynthetic pathway. For the past several years, we have obtained strong evidence showing the close relationship between SMP30, glucose metabolism disorder and non-alchoholic fatty liver disease in experiments with SMP30 knockout mice. Emerging proof links the following abnormalities: (i) the reduction of SMP30 by aging and/or excessive dietary fat or genetic deficiency causes a loss of Ca 2+ pumping activity, which impairs acute insulin release in pancreatic β-cells, initiates inflammatory responses with oxidative stress and endoplasmic reticulum stress in non-alchoholic steatohepatitis, exacerbates renal tubule damage, and introduces tubulointerstitial inflammation and fibrosis in diabetic nephropathy; (ii) vitamin C insufficiency also impairs acute insulin secretion in pancreatic β-cells by a mechanism distinct from that of the SMP30 deficiency; and (iii) the increased oxidative stress by concomitant deficiencies of SMP30, superoxide dismutase 1 and vitamin C similarly causes hepatic steatosis. Here, we review recent advances in our understanding of SMP30 in glucose metabolism disorder and non-alchoholic fatty liver disease. Geriatr Gerontol Int 2016; 16 (Suppl. 1): 4-16.Keywords: aging, diabetes mellitus, non-alchoholic fatty liver disease, senescence marker protein-30, vitamin C. Senescence marker protein-30 and its knockout miceSenescence marker protein-30 (SMP30) was first discovered in 1991 as an age-associated protein that decreased quantifiably in livers of aged rats.1,2 Thereafter, SMP30 proved to decrease in the liver, kidneys and lungs of mice during aging.3-5 Immunohistochemical analysis in the liver and primary cultured hepatocytes showed that SMP30 staining appeared in some, but not all, parenchymal cells, and localized in both the nuclei and cytoplasm.5 Furthermore, SMP30-positive cells localized mainly around the central veins in the livers of mice, and decreased numerically with aging.5 As established by reverse transcription polymerase chain reaction analysis, SMP30 transcripts were detected in not only the liver, kidneys and lungs of mice, but also in their brain, thymus, heart, testes and ovary; however, no SMP30 transcripts were identified in the spleen. 4,6 In humans, SMP30 was seen in parenchymal cells of the liver, proximal tubular cells of the kidney, acinal and ductal cells of the pancreas, and fasciculate cells of the adrenal cortex by applying immunohistochemical stain. 2,7 The human SMP30 gene is located in the p11.3-q11.2 segment of the X chromosome, 8 and its amino acid sequences are highly conserved among vertebrates. 7SMP30 knockout mice were established as a laboratory strain to clarify the physiological functions and the relationships bet...

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“…Counter to other aging observations, overexpression of SMP30 appears to cause bone loss and osteoporosis (22, 23). On the other hand, SMP30 deficiency leads to decreased glucose tolerance and abnormal lipid accumulation in the liver (22, 24–28). SMP30 has also been associated with control of cell proliferation and is down-regulated in human prostate and breast cancers (29, 30).…”

Section: Introductionmentioning

confidence: 99%

Senescence marker protein 30: functional and structural insights to its unknown physiological function

Scott

Bahnson

2011

BioMolecular Concepts

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Senescence marker protein 30 (SMP30) is a multifunctional protein involved in cellular Ca2+ homeostasis and the biosynthesis of ascorbate in non-primate mammals. The primary structure of the protein is highly conserved among vertebrates, suggesting the existence of a significant physiological function common to all mammals, including primates. Enzymatic activities of SMP30 include aldonolactone and organophosphate hydrolysis. Protective effects against apoptosis and oxidative stress have been reported. X-ray crystallography revealed that SMP30 is a six-bladed β-propeller with structural similarity to paraoxonase 1, another protein with lactonase and organophosphate hydrolase activities. SMP30 has recently been tied to several physiological conditions including osteoporosis, liver fibrosis, diabetes, and cancer. This review aims to describe the recent advances made toward understanding the connection between molecular structure, enzymatic activity and physiological function of this highly conserved, multifaceted protein.

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Decreased senescence marker protein-30 could be a factor that contributes to the worsening of glucose tolerance in normal aging

Abstract: To cite this article: Goji Hasegawa (2010) Decreased senescence marker protein-30 could be a factor that contributes to the worsening of glucose tolerance in normal aging, Islets, 2:4, 258-260,

Cited by 10 publications

References 17 publications

Frequency of impaired glucose tolerance and diabetes mellitus in subjects with fasting blood glucose below 6.1 mmol/L [110 mg/dL]

Frequency of impaired glucose tolerance and diabetes mellitus in subjects with fasting blood glucose below 6.1 mmol/L [110 mg/dL]

Involvement of senescence marker protein‐30 in glucose metabolism disorder and non‐alcoholic fatty liver disease

Senescence marker protein 30: functional and structural insights to its unknown physiological function

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