Lysosomal enzyme activities and RNA turnover rates in growing and nongrowing WI-38 and HeLa cells

In Vitro ◽  
1981 ◽  
Vol 17 (9) ◽  
pp. 816-824 ◽  
Author(s):  
Bratin K. Saha ◽  
Masazumi Sameshima ◽  
Fumiko Sameshima ◽  
David Schlessinger
Keyword(s):  
Hela Cells ◽  
Lysosomal Enzyme ◽  
Enzyme Activities ◽  
Rna Turnover ◽  
Turnover Rates

Disaccharidase and Lysosomal Enzyme Activities in Amniotic Fluid, Intestinal Mucosa and Meconium

Neonatology ◽  
1977 ◽  
Vol 32 (5-6) ◽  
pp. 280-289 ◽  
Author(s):  
I. Antonowicz ◽  
A. Milunsky ◽  
E. Lebenthal ◽  
H. Shwachman
Keyword(s):  
Amniotic Fluid ◽  
Intestinal Mucosa ◽  
Lysosomal Enzyme ◽  
Enzyme Activities

scholarly journals Proteolytische Aktivitäten der lysosomalen Enzyme bei Milchrindern* – 3. Mitteilung: Beziehungen der Energie- und Eiweißversorgung zur lysosomalen Enzymaktivität im Blutplasma beim Milchrind

2000 ◽  
Vol 43 (1) ◽  
pp. 17-26
Author(s):  
L. Panicke ◽  
J. Weingärtner ◽  
M. Schmidt ◽  
T. Król
Keyword(s):  
Enzyme Activity ◽  
Food Intake ◽  
Dairy Cows ◽  
Milk Production ◽  
Lysosomal Enzyme ◽  
Enzyme Activities ◽  
Correlation Coefficients ◽  
Food Ration ◽  
Milk Performance ◽  
Relationship Of

Abstract. Title of the paper: Relationship between lysosomal blood activity and milk content» of urea and protein in different phases of milk production in dairy cows Relationship of lysosomal enzyme activities in blood and supply of energy and protein in dairy cattle were investigated. Closed correlation coefficients were calculated for lysosomal enzyme activity and content of protein and urea in milk. Especially a high or a low content of protein in the food ration affects the lysosomal enzyme activities considerably. A different lysosomal response to equal food supply was gained after deviding the cow stock into different groups regarding performance at a different lactation status. Growth, breed, age, capacity of food intake and milk performance might be influencing factors.

Lysosomal enzyme activities of the bovine corneal endothelium

1986 ◽  
Vol 224 (4) ◽  
pp. 384-387 ◽  
Author(s):  
Satoshi Hara ◽  
Seiji Hayasaka ◽  
Katsuyoshi Mizuno
Keyword(s):  
Lysosomal Enzyme ◽  
Enzyme Activities ◽  
Corneal Endothelium

scholarly journals Urinary Lysosomal Enzyme Activities and Albuminuria in Ghanaian Patients with Type 2 Diabetes Mellitus

2016 ◽  
Vol 2016 ◽  
pp. 1-5 ◽  
Author(s):  
Henry Asare-Anane ◽  
Felix Twum ◽  
Emmanuel Kwaku Ofori ◽  
Erving L. Torgbor ◽  
Seth D. Amanquah ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Lysosomal Enzyme ◽  
Enzyme Activities ◽  
Renal Involvement ◽  
Fasting Blood Glucose ◽  
Urine Samples ◽  
Albumin Concentration ◽  
Spot Urine ◽  
Alanine Aminopeptidase

Renal tubular lysosomal enzyme activities like alanine aminopeptidase (AAP) and N-acetyl-β-D-glucosaminidase (NAG) have been shown to increase in patients developing diabetic nephropathy and nephrosclerosis. This study aimed to determine the activities of N-acetyl-β-D-glucosaminidase and alanine aminopeptidase and albumin concentration in urine samples of patients with type 2 diabetes. One hundred and thirty (65 type 2 diabetic and 65 nondiabetic) subjects participated in this study. Blood samples were drawn for measurements of fasting blood glucose, albumin (Alb), lipids, and creatinine (Cr). Early morning spot urine samples were also collected for activities of alanine aminopeptidase (AAP), N-acetyl-β-D-glucosaminidase (NAG), and concentration of albumin (U-Alb) and creatinine (U-Cr). Both NAG/Cr and AAP/Cr were significantly increased in diabetic subjects compared to controls (p<0.001). There was positive correlation between NAG/Cr and Alb/Cr (r=0.49,p<0.001) and between NAG/Cr and serum creatinine (r=0.441,p<0.001). A negative correlation was found between NAG/Cr and eGFR (r=-0.432,p<0.05). 9.3% and 12% of diabetics with normoalbuminuria had elevated levels of AAP/Cr and NAG/Cr, respectively. We conclude that measuring the urinary enzymes activities (NAG/Cr and AAP/Cr) could be useful as a biomarker of early renal involvement in diabetic complications.

scholarly journals Specific alterations in levels of mannose 6-phosphorylated glycoproteins in different neuronal ceroid lipofuscinoses

1998 ◽  
Vol 334 (3) ◽  
pp. 547-551 ◽  
Author(s):  
David E. SLEAT ◽  
Istvan SOHAR ◽  
Premila S. PULLARKAT ◽  
Peter LOBEL ◽  
Raju K. PULLARKAT
Keyword(s):  
Lysosomal Enzyme ◽  
Neurodegenerative Disorders ◽  
Enzyme Activities ◽  
Lysosomal Enzymes ◽  
Vesicular Transport ◽  
Cell Types ◽  
Neuronal Ceroid Lipofuscinoses ◽  
Mannose 6 Phosphate ◽  
Normal Controls ◽  
Lysosomal Proteins

Mannose 6-phosphate (Man-6-P) is a carbohydrate modification that is generated on newly synthesized lysosomal proteins. This modification is specifically recognized by two Man-6-P receptors that direct the vesicular transport of the lysosomal enzymes from the Golgi to a prelysosomal compartment. The Man-6-P is rapidly removed in the lysosome of most cell types; however, in neurons the Man-6-P modification persists. In this study we have examined the spectrum of Man-6-P-containing glycoproteins in brain specimens from patients with different neuronal ceroid lipofuscinoses (NCLs), which are progressive neurodegenerative disorders with established links to defects in lysosomal catabolism. We find characteristic alterations in the Man-6-P glycoproteins in specimens from late-infantile (LINCL), juvenile (JNCL) and adult (ANCL) patients. Man-6-P glycoproteins in LINCL patients were similar to controls, with the exception that the band corresponding to CLN2, a recently identified lysosomal enzyme whose deficiency results in this disease, was absent. In an ANCL patient, two Man-6-P glycoproteins were elevated in comparison with normal controls, suggesting that this disease also results from a perturbation in lysosomal hydrolysis. In JNCL, total levels of Man-6-P glycoproteins were 7-fold those of controls. In general this was reflected by increased lysosomal enzyme activities in JNCL but three Man-6-P glycoproteins were elevated to an even greater degree. These are CLN2 and the unidentified proteins that are also highly elevated in the ANCL.

Sign in / Sign up

Export Citation Format

Share Document