101662-5 Abnormal Prion Protein [Presence] in Cerebral spinal fluid by RT-QuIC

Term Description

Detection of pathologic prions in cerebrospinal fluid (CSF). The 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 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

LP435248-2   RT-QuIC
Real-time quaking-induced conversion (RT-QuIC) a technique to detect small amounts of PrPSc.. RT-QuIC test manipulates the ability of PrPSc to induce PrPC to misfold in a cyclical fashion to form aggregates of PrPSc fibrils, in real time by binding to a fluorescent dye, namely thioflavin T. Source: LOINC

Fully-Specified Name

Component

Prion protein.abnormal

Property

PrThr

Time

Pt

System

CSF

Scale

Ord

Method

RT-QuIC

Additional Names

Short Name

Abn Prion Prot CSF Ql RT-QuIC

Display Name

Abnormal Prion Protein RT-QuIC Ql (CSF)

Consumer Name Alpha Get Info

Abnormal prion protein, Spinal fluid

Basic Attributes

Class

CHEM

Type

Laboratory

First Released

Version 2.75

Last Updated

Version 2.75

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
• Chemistry
• 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.

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41027-4 Tau protein/Amyloid beta 42 peptide [Ratio] 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/Amyloid beta 42 peptide

Property

Ratio

Time

Pt

System

CSF

Scale

Qn

Method

Additional Names

Short Name

Tau Prot/AL beta42 CSF-Rto

Display Name

Tau protein/Amyloid beta 42 peptide (CSF) [Ratio]

Consumer Name Alpha Get Info

Tau protein/Amyloid Beta 42 Peptide, Spinal fluid

Basic Attributes

Class

CHEM

Type

Laboratory

First Released

Version 2.15

Last Updated

Version 2.73

Order vs. Observation

Both

Common Test Rank Get Info

14186

Member of these Panels

Language Variants Get Info

Related Names

• Ab42 peptide
• Abeta
• Abeta 42
• AL beta42
• Alzheimer disease
• Alzheimer's disease
• B
• Beta-amyloid
• Cerebral spinal fluid
• Cerebrospinal Fl
• Chemistry
• Neuro
• Neurology
• Pept
• Point in time
• PR
• Prot
• QNT
• Quan
• Quant
• Quantitative
• Random
• Ratios
• Rto
• Spinal Fl
• Spinal Fld
• Spinal Flu
• Spinal Fluid

33203-1 Amyloid beta 42 peptide [Mass/volume] in Cerebral spinal fluid

Part Descriptions

LP30823-6   Amyloid beta 42 peptide
Abeta 42 level is elevated in individuals whose chromosomes carry the genetic mutations characteristic of the early form of Alzheimer's. Source: Regenstrief Institute

LP30823-6   Amyloid beta 42 peptide
Amyloid beta (Aβ or Abeta) is a peptide of 36-43 amino acids that is processed from the Amyloid precursor protein. While it is most commonly known in association with Alzheimer's disease, it does not exist specifically to cause disease. Evidence has been found that Aβ has multiple non-disease activities.

The most common isoforms are Aβ40 and Aβ42; the shorter form is typically produced by cleavage that occurs in the endoplasmic reticulum, while the longer form is produced by cleavage in the trans-Golgi network. The Aβ40 form is the more common of the two, but Aβ42 is the more fibrillogenic and is thus associated with disease states. Mutations in APP associated with early-onset Alzheimer's have been noted to increase the relative production of Aβ42, and thus one suggested avenue of Alzheimer's therapy involves modulating the activity of β and γ secretases to produce mainly Aβ40.

Increases in either total Aβ levels or the relative concentration of both Aβ40 and Aβ42 (where the former is more concentrated in cerebrovascular plaques and the latter in neuritic plaques) have been implicated in the pathogenesis of both familial and sporadic Alzheimer's disease. Due to its more hydrophobic nature, the Aβ42 is the most amyloidogenic form of the peptide. 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, Wikipedia

Fully-Specified Name

Component

Amyloid beta 42 peptide

Property

MCnc

Time

Pt

System

CSF

Scale

Qn

Method

Additional Names

Short Name

AL beta42 CSF-mCnc

Display Name

Amyloid beta 42 peptide (CSF) [Mass/Vol]

Consumer Name Alpha Get Info

Amyloid beta 42 peptide, Spinal fluid

Basic Attributes

Class

CHEM

Type

Laboratory

First Released

Version 2.09

Last Updated

Version 2.73

Order vs. Observation

Both

Common Test Rank Get Info

17504

Member of these Panels

Language Variants Get Info

Related Names

• Ab42 peptide
• Abeta
• Abeta 42
• AL beta42
• Alzheimer disease
• Alzheimer's disease
• B
• Beta-amyloid
• Cerebral spinal fluid
• Cerebrospinal Fl
• Chemistry
• Level
• Mass concentration
• Pept
• Point in time
• QNT
• Quan
• Quant
• Quantitative
• Random
• Spinal Fl
• Spinal Fld
• Spinal Flu
• Spinal Fluid

Example Units

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

69048-7 Immunologist review of results

Fully-Specified Name

Component

Immunologist review

Property

Imp

Time

Pt

System

XXX

Scale

Nar

Method

Additional Names

Short Name

Immunologist review

Display Name

Immunologist review [Interp]

Consumer Name Alpha Get Info

Immunologist review of test result

Basic Attributes

Class

MISC

Type

Laboratory

First Released

Version 2.38

Last Updated

Version 2.75

Change Reason

Release 2.75: ORDER_OBS: submitter requested change;

Order vs. Observation

Both

Common Test Rank Get Info

4075

Member of these Panels

Language Variants Get Info

Related Names

• Impression
• Impression/interpretation of study
• Impressions
• Interp
• Interpretation
• Misc
• Miscellaneous
• Narrative
• Other
• Point in time
• Random
• Report
• Spec
• To be specified in another part of the message
• Unspecified