Ignet

Gene Information

Gene symbol: CPD

Gene name: carboxypeptidase D

HGNC ID: 2301

Synonyms: GP180

Related Genes

#	Gene Symbol	Number of hits
1	CPE	1 hits
2	INS	1 hits

Related Sentences

#	PMID	Sentence
1	21628999	Differential regulation and localization of carboxypeptidase D and carboxypeptidase E in human and mouse β-cells.
2	21628999	Defects in insulin processing enzymes including prohormone convertases 1/3 and 2, and carboxypeptidase E (CPE) can lead to β-cell stress and hyperproinsulinemia, both of which are features of type 2 diabetes.
3	21628999	Previously, we demonstrated that lipotoxicity led to the degradation of CPE, but did not affect its related enzyme, carboxypeptidase D (CPD).
4	21628999	In this study, we found that CPD was significantly up-regulated by elevated glucose, while CPE was not.
5	21628999	Low doses of insulin also increased CPD protein levels, consistent with a role for autocrine signaling.
6	21628999	Glucose and insulin did not affect CPD or CPE expression in an α-cell line.
7	21628999	Furthermore, insulin treatment altered the CPD sub-cellular localization, which was distinct from CPE.
8	21628999	Somewhat surprisingly, the loss of CPE did not affect the levels of CPD.
9	21628999	Knockdown of CPD exerted no effect on CPE protein levels.
10	21628999	In addition, while our previous study demonstrated that even modest reduction of CPE was sufficient to induce β-cell apoptosis, CPD knockdown did not affect cell viability.
11	21628999	Taken together, our data demonstrate that CPE and CPD are differentially localized, differentially regulated and unlikely to have compensatory functions in pancreatic β-cells.
12	21628999	Differential regulation and localization of carboxypeptidase D and carboxypeptidase E in human and mouse β-cells.
13	21628999	Defects in insulin processing enzymes including prohormone convertases 1/3 and 2, and carboxypeptidase E (CPE) can lead to β-cell stress and hyperproinsulinemia, both of which are features of type 2 diabetes.
14	21628999	Previously, we demonstrated that lipotoxicity led to the degradation of CPE, but did not affect its related enzyme, carboxypeptidase D (CPD).
15	21628999	In this study, we found that CPD was significantly up-regulated by elevated glucose, while CPE was not.
16	21628999	Low doses of insulin also increased CPD protein levels, consistent with a role for autocrine signaling.
17	21628999	Glucose and insulin did not affect CPD or CPE expression in an α-cell line.
18	21628999	Furthermore, insulin treatment altered the CPD sub-cellular localization, which was distinct from CPE.
19	21628999	Somewhat surprisingly, the loss of CPE did not affect the levels of CPD.
20	21628999	Knockdown of CPD exerted no effect on CPE protein levels.
21	21628999	In addition, while our previous study demonstrated that even modest reduction of CPE was sufficient to induce β-cell apoptosis, CPD knockdown did not affect cell viability.
22	21628999	Taken together, our data demonstrate that CPE and CPD are differentially localized, differentially regulated and unlikely to have compensatory functions in pancreatic β-cells.
23	21628999	Differential regulation and localization of carboxypeptidase D and carboxypeptidase E in human and mouse β-cells.
24	21628999	Defects in insulin processing enzymes including prohormone convertases 1/3 and 2, and carboxypeptidase E (CPE) can lead to β-cell stress and hyperproinsulinemia, both of which are features of type 2 diabetes.
25	21628999	Previously, we demonstrated that lipotoxicity led to the degradation of CPE, but did not affect its related enzyme, carboxypeptidase D (CPD).
26	21628999	In this study, we found that CPD was significantly up-regulated by elevated glucose, while CPE was not.
27	21628999	Low doses of insulin also increased CPD protein levels, consistent with a role for autocrine signaling.
28	21628999	Glucose and insulin did not affect CPD or CPE expression in an α-cell line.
29	21628999	Furthermore, insulin treatment altered the CPD sub-cellular localization, which was distinct from CPE.
30	21628999	Somewhat surprisingly, the loss of CPE did not affect the levels of CPD.
31	21628999	Knockdown of CPD exerted no effect on CPE protein levels.
32	21628999	In addition, while our previous study demonstrated that even modest reduction of CPE was sufficient to induce β-cell apoptosis, CPD knockdown did not affect cell viability.
33	21628999	Taken together, our data demonstrate that CPE and CPD are differentially localized, differentially regulated and unlikely to have compensatory functions in pancreatic β-cells.
34	21628999	Differential regulation and localization of carboxypeptidase D and carboxypeptidase E in human and mouse β-cells.
35	21628999	Defects in insulin processing enzymes including prohormone convertases 1/3 and 2, and carboxypeptidase E (CPE) can lead to β-cell stress and hyperproinsulinemia, both of which are features of type 2 diabetes.
36	21628999	Previously, we demonstrated that lipotoxicity led to the degradation of CPE, but did not affect its related enzyme, carboxypeptidase D (CPD).
37	21628999	In this study, we found that CPD was significantly up-regulated by elevated glucose, while CPE was not.
38	21628999	Low doses of insulin also increased CPD protein levels, consistent with a role for autocrine signaling.
39	21628999	Glucose and insulin did not affect CPD or CPE expression in an α-cell line.
40	21628999	Furthermore, insulin treatment altered the CPD sub-cellular localization, which was distinct from CPE.
41	21628999	Somewhat surprisingly, the loss of CPE did not affect the levels of CPD.
42	21628999	Knockdown of CPD exerted no effect on CPE protein levels.
43	21628999	In addition, while our previous study demonstrated that even modest reduction of CPE was sufficient to induce β-cell apoptosis, CPD knockdown did not affect cell viability.
44	21628999	Taken together, our data demonstrate that CPE and CPD are differentially localized, differentially regulated and unlikely to have compensatory functions in pancreatic β-cells.
45	21628999	Differential regulation and localization of carboxypeptidase D and carboxypeptidase E in human and mouse β-cells.
46	21628999	Defects in insulin processing enzymes including prohormone convertases 1/3 and 2, and carboxypeptidase E (CPE) can lead to β-cell stress and hyperproinsulinemia, both of which are features of type 2 diabetes.
47	21628999	Previously, we demonstrated that lipotoxicity led to the degradation of CPE, but did not affect its related enzyme, carboxypeptidase D (CPD).
48	21628999	In this study, we found that CPD was significantly up-regulated by elevated glucose, while CPE was not.
49	21628999	Low doses of insulin also increased CPD protein levels, consistent with a role for autocrine signaling.
50	21628999	Glucose and insulin did not affect CPD or CPE expression in an α-cell line.
51	21628999	Furthermore, insulin treatment altered the CPD sub-cellular localization, which was distinct from CPE.
52	21628999	Somewhat surprisingly, the loss of CPE did not affect the levels of CPD.
53	21628999	Knockdown of CPD exerted no effect on CPE protein levels.
54	21628999	In addition, while our previous study demonstrated that even modest reduction of CPE was sufficient to induce β-cell apoptosis, CPD knockdown did not affect cell viability.
55	21628999	Taken together, our data demonstrate that CPE and CPD are differentially localized, differentially regulated and unlikely to have compensatory functions in pancreatic β-cells.
56	21628999	Differential regulation and localization of carboxypeptidase D and carboxypeptidase E in human and mouse β-cells.
57	21628999	Defects in insulin processing enzymes including prohormone convertases 1/3 and 2, and carboxypeptidase E (CPE) can lead to β-cell stress and hyperproinsulinemia, both of which are features of type 2 diabetes.
58	21628999	Previously, we demonstrated that lipotoxicity led to the degradation of CPE, but did not affect its related enzyme, carboxypeptidase D (CPD).
59	21628999	In this study, we found that CPD was significantly up-regulated by elevated glucose, while CPE was not.
60	21628999	Low doses of insulin also increased CPD protein levels, consistent with a role for autocrine signaling.
61	21628999	Glucose and insulin did not affect CPD or CPE expression in an α-cell line.
62	21628999	Furthermore, insulin treatment altered the CPD sub-cellular localization, which was distinct from CPE.
63	21628999	Somewhat surprisingly, the loss of CPE did not affect the levels of CPD.
64	21628999	Knockdown of CPD exerted no effect on CPE protein levels.
65	21628999	In addition, while our previous study demonstrated that even modest reduction of CPE was sufficient to induce β-cell apoptosis, CPD knockdown did not affect cell viability.
66	21628999	Taken together, our data demonstrate that CPE and CPD are differentially localized, differentially regulated and unlikely to have compensatory functions in pancreatic β-cells.
67	21628999	Differential regulation and localization of carboxypeptidase D and carboxypeptidase E in human and mouse β-cells.
68	21628999	Defects in insulin processing enzymes including prohormone convertases 1/3 and 2, and carboxypeptidase E (CPE) can lead to β-cell stress and hyperproinsulinemia, both of which are features of type 2 diabetes.
69	21628999	Previously, we demonstrated that lipotoxicity led to the degradation of CPE, but did not affect its related enzyme, carboxypeptidase D (CPD).
70	21628999	In this study, we found that CPD was significantly up-regulated by elevated glucose, while CPE was not.
71	21628999	Low doses of insulin also increased CPD protein levels, consistent with a role for autocrine signaling.
72	21628999	Glucose and insulin did not affect CPD or CPE expression in an α-cell line.
73	21628999	Furthermore, insulin treatment altered the CPD sub-cellular localization, which was distinct from CPE.
74	21628999	Somewhat surprisingly, the loss of CPE did not affect the levels of CPD.
75	21628999	Knockdown of CPD exerted no effect on CPE protein levels.
76	21628999	In addition, while our previous study demonstrated that even modest reduction of CPE was sufficient to induce β-cell apoptosis, CPD knockdown did not affect cell viability.
77	21628999	Taken together, our data demonstrate that CPE and CPD are differentially localized, differentially regulated and unlikely to have compensatory functions in pancreatic β-cells.
78	21628999	Differential regulation and localization of carboxypeptidase D and carboxypeptidase E in human and mouse β-cells.
79	21628999	Defects in insulin processing enzymes including prohormone convertases 1/3 and 2, and carboxypeptidase E (CPE) can lead to β-cell stress and hyperproinsulinemia, both of which are features of type 2 diabetes.
80	21628999	Previously, we demonstrated that lipotoxicity led to the degradation of CPE, but did not affect its related enzyme, carboxypeptidase D (CPD).
81	21628999	In this study, we found that CPD was significantly up-regulated by elevated glucose, while CPE was not.
82	21628999	Low doses of insulin also increased CPD protein levels, consistent with a role for autocrine signaling.
83	21628999	Glucose and insulin did not affect CPD or CPE expression in an α-cell line.
84	21628999	Furthermore, insulin treatment altered the CPD sub-cellular localization, which was distinct from CPE.
85	21628999	Somewhat surprisingly, the loss of CPE did not affect the levels of CPD.
86	21628999	Knockdown of CPD exerted no effect on CPE protein levels.
87	21628999	In addition, while our previous study demonstrated that even modest reduction of CPE was sufficient to induce β-cell apoptosis, CPD knockdown did not affect cell viability.
88	21628999	Taken together, our data demonstrate that CPE and CPD are differentially localized, differentially regulated and unlikely to have compensatory functions in pancreatic β-cells.
89	21628999	Differential regulation and localization of carboxypeptidase D and carboxypeptidase E in human and mouse β-cells.
90	21628999	Defects in insulin processing enzymes including prohormone convertases 1/3 and 2, and carboxypeptidase E (CPE) can lead to β-cell stress and hyperproinsulinemia, both of which are features of type 2 diabetes.
91	21628999	Previously, we demonstrated that lipotoxicity led to the degradation of CPE, but did not affect its related enzyme, carboxypeptidase D (CPD).
92	21628999	In this study, we found that CPD was significantly up-regulated by elevated glucose, while CPE was not.
93	21628999	Low doses of insulin also increased CPD protein levels, consistent with a role for autocrine signaling.
94	21628999	Glucose and insulin did not affect CPD or CPE expression in an α-cell line.
95	21628999	Furthermore, insulin treatment altered the CPD sub-cellular localization, which was distinct from CPE.
96	21628999	Somewhat surprisingly, the loss of CPE did not affect the levels of CPD.
97	21628999	Knockdown of CPD exerted no effect on CPE protein levels.
98	21628999	In addition, while our previous study demonstrated that even modest reduction of CPE was sufficient to induce β-cell apoptosis, CPD knockdown did not affect cell viability.
99	21628999	Taken together, our data demonstrate that CPE and CPD are differentially localized, differentially regulated and unlikely to have compensatory functions in pancreatic β-cells.
100	21628999	Differential regulation and localization of carboxypeptidase D and carboxypeptidase E in human and mouse β-cells.
101	21628999	Defects in insulin processing enzymes including prohormone convertases 1/3 and 2, and carboxypeptidase E (CPE) can lead to β-cell stress and hyperproinsulinemia, both of which are features of type 2 diabetes.
102	21628999	Previously, we demonstrated that lipotoxicity led to the degradation of CPE, but did not affect its related enzyme, carboxypeptidase D (CPD).
103	21628999	In this study, we found that CPD was significantly up-regulated by elevated glucose, while CPE was not.
104	21628999	Low doses of insulin also increased CPD protein levels, consistent with a role for autocrine signaling.
105	21628999	Glucose and insulin did not affect CPD or CPE expression in an α-cell line.
106	21628999	Furthermore, insulin treatment altered the CPD sub-cellular localization, which was distinct from CPE.
107	21628999	Somewhat surprisingly, the loss of CPE did not affect the levels of CPD.
108	21628999	Knockdown of CPD exerted no effect on CPE protein levels.
109	21628999	In addition, while our previous study demonstrated that even modest reduction of CPE was sufficient to induce β-cell apoptosis, CPD knockdown did not affect cell viability.
110	21628999	Taken together, our data demonstrate that CPE and CPD are differentially localized, differentially regulated and unlikely to have compensatory functions in pancreatic β-cells.