help button home button Endocrine Society Endocrinology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Endocrinology, doi:10.1210/en.2004-0780
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
145/12/5465    most recent
Author Manuscript (PDF)
Right arrow Purchase Article
Right arrow View Shopping Cart
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Request Copyright Permission
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Khurana, R.
Right arrow Articles by Madhusudan, K. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Khurana, R.
Right arrow Articles by Madhusudan, K. P.
Endocrinology Vol. 145, No. 12 5465-5470
Copyright © 2004 by The Endocrine Society

BRIEF COMMUNICATION

Unraveling the Amyloid Associated with Human Medullary Thyroid Carcinoma

Ritu Khurana, Amit Agarwal, Virendra K. Bajpai, Nidhi Verma, Ashok K. Sharma, Ram P. Gupta and Kunnath P. Madhusudan

Molecular and Structural Biology Division (R.K., N.V.), Electron Microscopy Unit (V.K.B.), Sophisticated Analytical Instrument Facility (K.P.M.), Central Drug Research Institute, Chattar Manzil Building, Lucknow 226001; and Department of Endocrine Surgery (A.A.), Sanjay Gandhi Post Graduate Institute, Lucknow 226014; and Central Electronics and Engineering Research Institute (A.K.S., R.P.G.), Pilani 333031, India

Address all correspondence and requests for reprints to: Dr. Ritu Khurana, Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500007, India. E-mail: rkhurana{at}ccmb.res.in.

Medullary thyroid carcinoma (MTC) is associated with amyloid deposition in the surrounding tissues. MTC-positive tumor thyroid tissues surgically removed from patients were used in our study to extract amyloid. We tested the MTC extracts for the presence of amyloid by measuring fold enhancement of thioflavin T fluorescence. Transmission electron microscopic study and atomic force microscopy of MTC patient extracts revealed typical amyloid fibrils. Matrix-assisted laser desorption ionization-time of flight mass spectrometric analysis demonstrated full-length calcitonin as the constituent of the MTC amyloid from seven patients. Our results unequivocally demonstrated that full-length calcitonin is the sole constituent of amyloid in MTC.




This article has been cited by other articles:


Home page
 FASEB J.Home page
E. Herczenik and M. F. B. G. Gebbink
Molecular and cellular aspects of protein misfolding and disease
FASEB J, July 1, 2008; 22(7): 2115 - 2133.
[Abstract] [Full Text] [PDF]

Home page
 ChestHome page
W. Y. Lee and R. A. Balk
Diffuse Pulmonary Nodules in a 25-Year-Old Man With Diarrhea and Weight Loss
Chest, May 1, 2008; 133(5): 1252 - 1255.
[Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Lin, M.-C. Chen, C.-Y. Chiu, Y.-M. Song, and S.-Y. Lin
Cdk5 Regulates STAT3 Activation and Cell Proliferation in Medullary Thyroid Carcinoma Cells
J. Biol. Chem., February 2, 2007; 282(5): 2776 - 2784.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Endocrinology Endocrine Reviews J. Clin. End. & Metab.
Molecular Endocrinology Recent Prog. Horm. Res. All Endocrine Journals
Copyright © 2004 by The Endocrine Society