Amyloid Protein Identification, Paraffin (AMPIP), Amyloid Protein Identification, Paraffin, LC-MS/MS (AMPIP), GPAMYPROPAR, GPMSCBB, GPMSCBB, Amyloid AA, Amyloid AL, Amyloid ATTR, Amyloid LECT-2, Amyloid
Definitive identification of amyloid proteins
AMYLOID:
Formalin-fixed or B5-fixed, paraffin-embedded tissue block
Preliminary pathology report and history are required.
A brief explanatory note or consultative letter is also recommended
Collection Instructions: Do not send fixed tissue slides. Testing can only be done on paraffin-embedded tissue blocks.
Shipping Instructions: Attach the green pathology address label included in the kit to the outside of the transport container.
Reject
No significant cautionary statements.
Amyloidosis is a group of hereditary and acquired diseases that are unified by extracellular tissue deposition of misfolded proteins resulting in end organ damage. Amyloidosis can be a systemic or localized disease. Although many cases of amyloidosis are hereditary, most are acquired as the result of an underlying monoclonal B-cell/plasma cell malignancy, as a phenomenon of aging, or as the result of long-standing chronic inflammation. Specific amyloid-related diseases are therefore associated with specific amyloid proteins. These include kappa or lambda immunoglobulin light chains (AL amyloid), transthyretin (ATTR amyloid), serum amyloid A (SAA amyloid), and other uncommon subtypes. Because treatment of amyloidosis patients differs radically for the different amyloid subtypes, it is critically important to accurately identify the proteins that constitute the amyloid deposits.
The basic diagnosis of amyloidosis is typically achieved by Congo red staining of paraffin-embedded tissue biopsy specimens obtained from diverse anatomic sites and demonstrating Congo red-positive, apple-green birefringent, amyloid deposits in the tissues. The next step is to definitively subtype the amyloid deposits. This test fulfills that need. It relies on laser microdissection of Congo red-positive amyloid deposits followed by analysis by liquid chromatography-tandem mass spectrometry to accurately determine the identity of the proteins that constitute the amyloid.
An interpretation will be provided.