97503-7 Abnormal Prion Protein [Presence] in Cerebral spinal fluid

Term Description

Detection of pathologic prions in cerebrospinal fluid (CSF). The submitter's test uses recombinant prion protein (PrP) as a reagent substrate and patient CSF in a real-time quaking-induced conversion (RT-QuIC) assay. If pathologic prions are present in the patient's CSF, they propagate misfolding of the reagent PrP to form amyloid, which is detected using a fluorescent indicator. RT-QuIC has been adopted in clinical practice due to the sensitivity, specificity, and use of CSF (not a brain biopsy) for testing. The submitter's reported sensitivity of RT-QuIC in detecting CJD is >90%, and the specificity approaches 100%.
Source: Regenstrief LOINC

Part Descriptions

LP35078-2   Prion protein.abnormal
Transmissible spongiform encephalopathies (TSEs), also known as prion diseases, are a group of progressive conditions (encephalopathies) that affect the brain and nervous system of many animals, including humans. According to the most widespread hypothesis they are transmitted by abnormal prions, though some other data suggest an involvement of a Spiroplasma infection. Mental and physical abilities deteriorate and a myriad of tiny holes appear in the cortex causing it to appear like a sponge (hence spongiform) when brain tissue obtained at autopsy is examined under a microscope. The disorders cause impairment of brain function, including memory changes, personality changes and problems with movement that worsen over time. Most TSEs are sporadic and occur in animals. Prion diseases of animals in include classical bovine spongiform encephalopathy (BSE) (C-type), atypical (H or L-type) BSE, Scrapie, atypical scrapie, Nor98, and chronic wasting disease (CWE). H-type and L-type BSE were named based on abnormal prion bands migrating to a higher (H) or lower (L) position on western blot analysis compared to the classical BSE (C-type) prion protein. Prion diseases of humans include classic Creutzfeldt-Jakob disease, new variant Creutzfeldt-Jakob disease (nvCJD, a human disorder related to Bovine spongiform encephalopathy), Gerstmann-Sträussler-Scheinker syndrome, fatal familial insomnia and kuru. These conditions form a spectrum of diseases with overlapping signs and symptoms. Copyright Text is available under the Creative Commons Attribution/Share-Alike License. See http://creativecommons.org/licenses/by-sa/3.0/ for details. Source: Wikipedia, Transmissible spongiform encephalopathy

Fully-Specified Name

Component

Prion protein.abnormal

Property

PrThr

Time

Pt

System

CSF

Scale

Ord

Method

Additional Names

Short Name

Abn Prion Prot CSF Ql

Display Name

Abnormal Prion Protein Ql (CSF)

Consumer Name Alpha Get Info

Abnormal prion protein, Spinal fluid

Basic Attributes

Class

MICRO

Type

Laboratory

First Released

Version 2.70

Last Updated

Version 2.71

Order vs. Observation

Both

Example Answer List LL2038-9

Member of these Panels

Language Variants Get Info

Related Names

• abn
• Abn Prion Prot
• abnorm
• Bovine spongiform encephalopathy
• BSE
• Cerebral spinal fluid
• Cerebrospinal Fl
• ID
• Infectious Disease
• InfectiousDisease
• Microbiology
• Neuro
• Neurology
• Ordinal
• Point in time
• PR
• Prot
• PrP
• QL
• Qual
• Qualitative
• Random
• Scrapie
• Screen
• Spinal Fl
• Spinal Fld
• Spinal Flu
• Spinal Fluid

Third Party Copyright

This material includes SNOMED Clinical Terms® (SNOMED CT®) which is used by permission of the International Health Terminology Standards Development Organisation (IHTSDO) under license. All rights reserved. SNOMED CT® was originally created by The College of American Pathologists. "SNOMED" and "SNOMED CT" are registered trademarks of the IHTSDO.

This material includes content from the US Edition to SNOMED CT, which is developed and maintained by the U.S. National Library of Medicine and is available to authorized UMLS Metathesaurus Licensees from the UTS Downloads site at https://uts.nlm.nih.gov.

Use of SNOMED CT content is subject to the terms and conditions set forth in the SNOMED CT Affiliate License Agreement. It is the responsibility of those implementing this product to ensure they are appropriately licensed and for more information on the license, including how to register as an Affiliate Licensee, please refer to http://www.snomed.org/snomed-ct/get-snomed-ct or info@snomed.org<mailto:info@snomed.org>. This may incur a fee in SNOMED International non-Member countries.

30160-6 Tau protein [Mass/volume] in Cerebral spinal fluid

Part Descriptions

LP28537-6   Tau protein
CSF tau phosphorylated at threonine 181 (p-tau181) is a widely used biomarker for Alzheimer disease (AD) and has recently been regarded to reflect β-amyloid and/or p-tau deposition in the AD brain. Neuronal intranuclear inclusion disease (NIID) is a neurodegenerative disease characterized by intranuclear inclusions in neurons, glial cells, and other somatic cells. Symptoms include dementia, neuropathy, and others. CSF biomarkers were not reported. The objective of this study was to investigate whether CSF biomarkers including p-tau181 are altered in patients with NIID. Source: Máxima MC

LP28537-6   Tau protein
Tau proteins are proteins that stabilize microtubules. They are abundant in neurons of the central nervous system and are less common elsewhere, but are also expressed at very low levels in CNS astrocytes and oligodendrocytes. When tau proteins are defective, and no longer stabilize microtubules properly, they can result in dementias such as Alzheimer's disease.

Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation.

Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene.

Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization Taniguchi et al., 2001. Copyright Text is available under the Creative Commons Attribution/Share-Alike License. See http://creativecommons.org/licenses/by-sa/3.0/ for details. Source: Wikipedia, Tau protein

Fully-Specified Name

Component

Tau protein

Property

MCnc

Time

Pt

System

CSF

Scale

Qn

Method

Additional Names

Short Name

Tau Prot CSF-mCnc

Display Name

Tau protein (CSF) [Mass/Vol]

Consumer Name Alpha Get Info

Tau protein, Spinal fluid

Basic Attributes

Class

CHEM

Type

Laboratory

First Released

Version 2.04

Last Updated

Version 2.73

Order vs. Observation

Both

Common Test Rank Get Info

18045

Member of these Panels

Member of these Groups Get Info

Language Variants Get Info

Related Names

• Alzheimer disease
• Alzheimer's disease
• Cerebral spinal fluid
• Cerebrospinal Fl
• Chemistry
• Level
• Mass concentration
• Neuro
• Neurology
• Point in time
• PR
• Prot
• QNT
• Quan
• Quant
• Quantitative
• Random
• Spinal Fl
• Spinal Fld
• Spinal Flu
• Spinal Fluid

Example Units

31989-7 14-3-3 Ag [Presence] in Cerebral spinal fluid

Part Descriptions

LP36860-2   14-3-3
The 14-3-3 protein is a highly conserved family of proteins that was originally found in brain tissue in 1968. There are seven isoforms of 14-3-3 protein in mammals which are found in all eukaryotic cells. The proteins weigh between 25 and 30 kilo Daltons and interact with more than 200 target proteins. 14-3-3 proteins are able to easily move between the cytoplasm and the nucleus but are mainly found in the cytoplasm. 14-3-3 is an important regulator of cellular function including controlling the cycle of the cell, cell growth, differentiation, survival, apoptosis, migration and spreading. The isoform 14-3-3o is believed to have a role in human cancer development. PMID: 15857577 Source: Regenstrief LOINC

Fully-Specified Name

Component

14-3-3 Ag

Property

PrThr

Time

Pt

System

CSF

Scale

Ord

Method

Additional Names

Short Name

14-3-3 Ag CSF Ql

Display Name

14-3-3 Ag Ql (CSF)

Consumer Name Alpha Get Info

14-3-3 antigen, Spinal fluid

Basic Attributes

Class

SERO

Type

Laboratory

First Released

Version 2.07

Last Updated

Version 2.73

Change Reason

The PrThr property is used for LOINC terms whose results are reported using an ordered categorical scale, regardless of whether or not an internal threshold was used to make that determination. This change was approved by the Laboratory LOINC Committee in June 2016.

Order vs. Observation

Both

Common Test Rank Get Info

15484

Member of these Panels

Member of these Groups Get Info

Language Variants Get Info

Related Names

• Antigen
• Antigens
• Cerebral spinal fluid
• Cerebrospinal Fl
• CJ
• CJD
• Creutzfeldt-Jacob Disease
• Creutzfeldt-Jakob Disease
• III
• Ordinal
• Point in time
• PR
• QL
• Qual
• Qualitative
• Random
• Screen
• Serology
• Spinal Fl
• Spinal Fld
• Spinal Flu
• Spinal Fluid