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The following primary phospho and non-phospho antibodies were used for IB analysis, SMN (610647, BD Biosciences), γH2AX (pSer 139) (NB100-79967), H2AX (NBP2-27428) and CHK1 (NB100-1768) from Novus Biologicals, ATM and p-CHK1 (Ser345) (2348) from Cell Signaling, β-actin (A5316) and α-tubulin (T8203) from Sigma-Aldrich, CHK2 (AFFN-CHEK2-17D2) deposited to DHSB by EU Program Affinomics), p-CHK2 (Thr68) (bs-3721R, Bioss Antibodies), p-BRCA1 (Ser1423) (ab90528), p-DNAPKcs (Ser2056) (ab18192), total-DNAPKcs (ab53701) and p-ATM (Ser1981) (ab81292) from Abcam, p-ATR (Ser 428) (sc-109912), BRCA1 (sc-642) (SantaCruz Biotech), ATR (ab-428) (Genescript) and SETX (#ab220827, Abcam).

Total RNA was isolated from cultured (i) HeLa cells that were untransfected (Control) or transfected with siRNA 100 nM) against SMN1 or scrambled siRNA sequence (Scramble) and incubated for 30 h and (ii) normal (non-SMA) dividing human cells, WI-38 and GM03814, and SMA patient cells, GM03813 and GM09677 (SMA) using RNase Mini Kit (Qiagen). Total RNA (100 ng) per sample was reverse-transcribed using SuperScript VILO Kit (Invitrogen). We used SYBR Green PCR Master Mix (Applied Biosystems) for real-time quantitative polymerase chain reaction (RT-qPCR) analysis. The relative mRNA expression levels were calculated using log2 −ΔΔCT method ( 14 ). The glyceraldehyde-3-phosphate dehydrogenase ( GAPDH ) gene was used as a positive control. The primer sequences were as follows: GAPDH primers: forward, 5′- ATAGGCGAGATCCCTCCAA-3′; reverse, 5′- TGAAGACGCCAGTGGAC-3′, SETX primers, forward 5′-CTTCATCCTCGGACATTTGAG-3′; and reverse 5′-TTAATAATGGCACCACGCTTC-3′ ( 24 ) and DNA-PKcs primers, forward 5′-CATCCAGAGTAGCGAATACTTCC-3′, reverse 5′-TTGTTTCGCAACCAGTTCAC-3′ ( 25 ).

Cells cultured on glass coverslips were washed with phosphate-buffered saline (PBS) and fixed in pre-chilled methanol (−20°C) for 5 min followed by 2 min in pre-chilled acetone (−20°C) at −20°C ( 20 ). Cells were also fixed with 4% PFA as described in individual experimental sections. PFA fixed cells were washed with PBS, permeabilized by incubation with 0.1% Triton-X100 for 5 min and washed 3× with PBS. Cells were blocked with 3% BSA in PBS with 0.5% Tween 20 (PBS-T) for 30 min at room temperature ( 22 ). Dividing cells were double labeled by sequential incubation with primary antibody against SMN for 1 h, washed 3× with PBS-T for 5 min and incubated with secondary antibody Alexa488-conjugated anti-mouse IgG, washed 3× with PBS-T for 5 min and followed by staining with second primary antibody against either one of the markers for nuclear bodies, p80 Coilin (#NBP2-15939, Novus Biologicals), LSM11 (#NBP1-81938, Novus Biologicals) and PML (#PM001, MBL) or DDR markers, γH2AX (#ab26350, Abcam), 53BP1 (#4937, Cell Signaling), p-ATM, p-ATR, p-CHK1, p-CHK2, p-DNAPKcs, p-BRCA1 or RNA–DNA hybrid (Clone #S9.6) (#ENH001, Kerafast) or SETX (#ab220827) or RNA Pol II (#ab210527), RNA helicase A (RHA) (#ab26271) and p-RPA32/RPA2 (Thr21) (#ab109394) from Abcam, for 1 h, washed 3× with PBS-T for 5 min, incubated with secondary antibody Alexa594-conjugated anti-rabbit IgG, washed 3× with PBS-T for 5 min. For ribonuclease H (RNase H) enzyme treatment, control and siSMN transfected cells were extracted with CSK buffer containing 0.1% Triton X-100 for 5 min followed by washing with CSK buffer without Triton-X100. Cells were incubated in RNase H digestion buffer (20 mM HEPES, pH 8.0, 50 mM KCl, 4 mM MgCl 2 , 1 mM 1, 4-dithiothreitol (DTT), 50 μg/ml BSA, ∼10U RNase H/ml) for 20 min at 37°C ( 26 ). After RNAse H treatment cells were washed with PBS and fixed in 4% PFA and double stained for SMN and coilin. Processed coverslips were mounted on microscope slides with Vectashield mounting medium containing DAPI and edges sealed with a coat of clear nail polish.


You need to find out the cause of your B12 deficiency. You should be tested for pernicious anemia before taking any B12. I’d be cautious about getting this tested after starting on B12 as it can interfere with the test results.

Do you have any of these other B12 deficiency risks: vegetarian/vegan, used PPIs or H2 blockers, take Metformin, had nitrous oxide anesthesia for surgery or dental work, gastric surgery?

If you have pernicious anemia you will need treatment for life.

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How many micrograms are in the tablets and are they dissolved under your tongue?

Rule of thumb is, you are on them for life. If you reach your mark and stop taking them, two things can happen, your levels will stay the same, as far as you know between doctor visits, and of course, it depends on what your doctor considers the right level, or, your levels can go down. Believe me, it’s far better to take b12 for life than to chance having the things happen to you that can happen to you when it’s too low. The pills are extremely safe. Don’ t chance it.

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gaurav says

hi I am having severe vitamin b12 deficiency.(167) my doctor prescribed me cyanocobalamin (vitcofol). but i would like to take methylcobalamin instead. Is it ok. also can you tell me how to self inject methylcobalamin by syringe. thanks in advance.

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Michael Lim says

I did a little researcg on this before and this is what I understand: If you have a high concentration of mercury in your system, methylcobalamin isn’t advisable. This will react with mercury and produce methyl mercury, which is worse as it is more reactive biologically. Perhaps someone else can shed more light on this.

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Frank says

There are loads of sources of the methyl group, almost all of them in higher concentrations than you’ll get from MeCobalamin. 1000ug of MeCB will produce just 11ug of methyl radicals. That’s about one thousandth the amount of methyl in a glss of red wine.


Brandon says

Systematic analysis of an extended sample of the patient's spontaneous (propositional) speech ( Table 2 ) is the single most valuable aspect of the examination. Where little spontaneous conversation is offered, the patient can be asked to describe a scene in a photograph or drawing (an example is shown in Fig. 4 A). This is preferable to asking the patient to recount an event in their daily routine, as it allows speech to be evaluated independently of episodic memory and provides a standard with which to compare speech characteristics in different clinical situations. Examples of scene descriptions produced by patients with canonical speech disorders are presented in Table 3 . Valuable information is often obtained from observing the patient's general behaviour and approach to the clinical interview. The inert patient with a frontal dementia, who offers little speech at all and sits passively throughout the interview, makes a very different impression from the patient with PNFA, who is obviously frustrated by their difficulties and struggles to compensate with an excess of non-verbal gestures, and both contrast with the garrulous patient with semantic dementia (SD), who produces a steady stream of circumlocutory speech.

Fig. 4
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Materials for assessing speech at the bedside. (Reproduced with permission of Professor EK Warrington.) ( A ) A beach scene, illustrating one means of eliciting conversational speech (see examples in Table 3 ). ( B ) A passage for reading aloud (see text).

Fig. 4
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Materials for assessing speech at the bedside. (Reproduced with permission of Professor EK Warrington.) ( A ) A beach scene, illustrating one means of eliciting conversational speech (see examples in Table 3 ). ( B ) A passage for reading aloud (see text).

The classification of aphasias as ‘expressive’ or ‘receptive’ (or ‘motor’ or ‘sensory’) is both overly simplistic and inaccurate (Geschwind, 1971 ): few patients present with either a pure speech production or comprehension deficit. This is true for acute lesions (Brust et al ., 1976 ), but particularly relevant to the categorization of the progressive aphasias. Similarly, classifying speech disturbances as ‘fluent’ or ‘non-fluent’ also oversimplifies the clinical phenomenology and is open to misinterpretation. Fluency describes the flow of speech output, but it is multidimensional: ‘non-fluency’ may be due to a number of different factors, including decreased phrase length, agrammatism, poor articulation or slower speech rate (Hillis, 2007 ). As these impairments tend to occur together, an individual patient's speech can often be reliably categorized as fluent or non-fluent; moreover, certain dimensions (particular motor aspects such as rate and articulation) make a relatively greater contribution to the impression of dysfluency. However, the component processes are dissociable: thus, patients with milder forms of ‘non-fluent’ speech may still produce relatively long phrases or sentences, albeit containing many errors. Even in more advanced cases of ‘non-fluent’ speech, there may be stereotyped phrases comprising several words (e.g. ‘Hello, how are you?’): such phrases can be regarded as an expressive ‘unit’ serving a similar function to a single word. Conversely, patients with ‘fluent’ aphasias generally have empty speech due to an impaired ability to find appropriate content words but commonly also have conversational pauses during which they struggle to find the appropriate word: these gaps tend to reduce the overall number of words produced (‘logopenia’) and thus the fluency of the utterance as a whole. Although it remains clinically useful as a descriptive term, ‘fluency’ is therefore potentially misleading as a criterion for the categorization of speech and language syndromes, which is more usefully based on a combination of features ( Fig. 2 ).

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